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Volumn 2, Issue 5, 1997, Pages 546-556

Protein monolayers at interfaces

Author keywords

A w air water; AFM atomic force microscopy; AMP ATP adenosine mono triphosphate; ATR attenuated total reflection; C1q or C3 complement factors 1q or 3; CD circular dichroism; CV cyclic voltammetry; Cyt cytochrome; EM electron microscope microscopy

Indexed keywords


EID: 0039054420     PISSN: 13590286     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0286(97)80043-5     Document Type: Article
Times cited : (35)

References (159)
  • 1
    • 0030949157 scopus 로고    scopus 로고
    • Protein arrays: Concepts and subjects
    • K. Nagayerna, Ebashi G. Japan Scientific Societies Press/Elsevier, Tokyo/Limerick, Comprehensive review on current directions of research with protein monolayers in materials research including 192 references
    • Nagayama K. Protein arrays: concepts and subjects. Nagayerna K, Ebashi G. Protein array: an alternate biomolecular system. 34:1997;3-23 Japan Scientific Societies Press/Elsevier, Tokyo/Limerick, Comprehensive review on current directions of research with protein monolayers in materials research including 192 references.
    • (1997) Protein Array: An Alternate Biomolecular System , vol.34 , pp. 3-23
    • Nagayama, K.1
  • 2
    • 0029696595 scopus 로고    scopus 로고
    • Biological adhesion at interfaces
    • Comprehensive review of protein interaction with interfaces with a strong bias toward life science aspects including 129 references.
    • Hammer DA, Tirrell M. Biological adhesion at interfaces. Annu Rev Mater Sci. 26:1996;651-691 Comprehensive review of protein interaction with interfaces with a strong bias toward life science aspects including 129 references.
    • (1996) Annu Rev Mater Sci , vol.26 , pp. 651-691
    • Hammer, D.A.1    Tirrell, M.2
  • 3
    • 0030569732 scopus 로고    scopus 로고
    • Supported membranes - scientific and practical applications
    • Describes supported membranes as model systems to study protein interactions with biomembranes and protein diffusion within biomembranes. Emphasis is on biophysical concepts (includes 57 references).
    • Sackmann E. Supported membranes - scientific and practical applications. Science. 271:1996;43-48 Describes supported membranes as model systems to study protein interactions with biomembranes and protein diffusion within biomembranes. Emphasis is on biophysical concepts (includes 57 references).
    • (1996) Science , vol.271 , pp. 43-48
    • Sackmann, E.1
  • 4
    • 0030233185 scopus 로고    scopus 로고
    • Use of planar lipid monolayers for 2D crystallisation of proteins and simple analysis of specific lipid - Peptide interactions
    • Newman RH, Freemont PS. Use of planar lipid monolayers for 2D crystallisation of proteins and simple analysis of specific lipid - peptide interactions. Thin Solid Films. 284/285:1996;18-23.
    • (1996) Thin Solid Films , vol.284-285 , pp. 18-23
    • Newman, R.H.1    Freemont, P.S.2
  • 6
    • 0343807399 scopus 로고    scopus 로고
    • The pulmonary surfactant system - bioloscal functions, components, physicochemical properties and alterations during lung disease
    • Pison U, Herold R, Schürch S. The pulmonary surfactant system - bioloscal functions, components, physicochemical properties and alterations during lung disease. Colloid Surf A. 114:1996;165-184.
    • (1996) Colloid Surf a , vol.114 , pp. 165-184
    • Pison, U.1    Herold, R.2    Schürch, S.3
  • 8
    • 0030949159 scopus 로고    scopus 로고
    • Electron crystallography of macromolecular periodic arrays on phospholipid monolayers
    • K. Nagayama, Ebashi G. Tokyo/Limerick: Japan Scientific Societies Press/Elsevier. (Series Editor): Advances in Biophysics
    • Chiu W, Avial-Sakar AJ, Schmid MF. Electron crystallography of macromolecular periodic arrays on phospholipid monolayers. Nagayama K, Ebashi G. Protein array: an alternate biomolecular system. 34:1997;161-172 Japan Scientific Societies Press/Elsevier, Tokyo/Limerick. (Series Editor): Advances in Biophysics.
    • (1997) Protein Array: An Alternate Biomolecular System , vol.34 , pp. 161-172
    • Chiu, W.1    Avial-Sakar, A.J.2    Schmid, M.F.3
  • 9
    • 0001367472 scopus 로고    scopus 로고
    • QCM operation in liquids - constant sensitivity during formation of extended protein multilayers by affinity
    • Rickert J, Brecht A, Gopal W. QCM operation in liquids - constant sensitivity during formation of extended protein multilayers by affinity. Anal Chem. 69:1997;1441-1448.
    • (1997) Anal Chem , vol.69 , pp. 1441-1448
    • Rickert, J.1    Brecht, A.2    Gopal, W.3
  • 10
    • 0030977384 scopus 로고    scopus 로고
    • Supramolecular architectures for the functionalization of solid surfaces
    • K. Nagayama, Ebashi G. Tokyo/Limerick: Japan Scientific Societies Press/Elsevier. (Series Editor): Advances in Biophysics
    • Knoll W, Liley M, Piscevic D, Spinke J, Tarlov MJ. Supramolecular architectures for the functionalization of solid surfaces. Nagayama K., Ebashi G. Protein array: an alternate biomolecular system. 34:1997;231-251 Japan Scientific Societies Press/Elsevier, Tokyo/Limerick. (Series Editor): Advances in Biophysics.
    • (1997) Protein Array: An Alternate Biomolecular System , vol.34 , pp. 231-251
    • Knoll, W.1    Liley, M.2    Piscevic, D.3    Spinke, J.4    Tarlov, M.J.5
  • 12
  • 13
    • 0029708566 scopus 로고    scopus 로고
    • Formation of ultrathin polymer layers on solid substrates by means of polymerization-induced epitaxy and alternate adsorption
    • Sano M, Lvov Y, Kunitake T. Formation of ultrathin polymer layers on solid substrates by means of polymerization-induced epitaxy and alternate adsorption. Annu Rev Mater Sci. 26:1996;153-187.
    • (1996) Annu Rev Mater Sci , vol.26 , pp. 153-187
    • Sano, M.1    Lvov, Y.2    Kunitake, T.3
  • 14
    • 0029724374 scopus 로고    scopus 로고
    • Surface treatments of polymers for biocompatibility
    • Elbert DL, Hubbell JA. Surface treatments of polymers for biocompatibility. Annu Rev Mater Sci. 26:1996;365-394.
    • (1996) Annu Rev Mater Sci , vol.26 , pp. 365-394
    • Elbert, D.L.1    Hubbell, J.A.2
  • 15
    • 0001645664 scopus 로고    scopus 로고
    • Interfacial aspects of biomineralization
    • Hunter GK. Interfacial aspects of biomineralization. Curr Opin Solid State Mater Sci. 1:1996;430-435.
    • (1996) Curr Opin Solid State Mater Sci , vol.1 , pp. 430-435
    • Hunter, G.K.1
  • 16
    • 0030218457 scopus 로고    scopus 로고
    • The 'new' science of 'Complex Fluids'
    • Gelbart WM, Ben-Shaul A. The 'new' science of 'Complex Fluids'. J Phys Chem. 100:1996;13169-13189.
    • (1996) J Phys Chem , vol.100 , pp. 13169-13189
    • Gelbart, W.M.1    Ben-Shaul, A.2
  • 17
    • 0030234522 scopus 로고    scopus 로고
    • Layer formation of a lipid-tagged single-chain antibody and the interaction with antigen
    • Vikholm I, Peltonen J. Layer formation of a lipid-tagged single-chain antibody and the interaction with antigen. Thin Solid Films. 284/285:1996;924-926.
    • (1996) Thin Solid Films , vol.284-285 , pp. 924-926
    • Vikholm, I.1    Peltonen, J.2
  • 18
    • 0030156231 scopus 로고    scopus 로고
    • Incorporation of lipid-tagged single-chain antibodies into lipid monolayers and the interaction with antigen
    • Vikholm I, Gyorvary E, Peltonen J. Incorporation of lipid-tagged single-chain antibodies into lipid monolayers and the interaction with antigen. Langmuir. 12:1996;3276-3281.
    • (1996) Langmuir , vol.12 , pp. 3276-3281
    • Vikholm, I.1    Gyorvary, E.2    Peltonen, J.3
  • 19
    • 0000592630 scopus 로고    scopus 로고
    • Formation and characterization of lipopeptide layers at interfaces for the molecular recognition of antibodies
    • A complete study of antibody binding to a lipid-bound peptide segment of the picorna virus capsid protein VP1 at the air/water interface, after transfer to solid substrates, and in SUV's using CD, FTIR, SPM and FM is given.
    • Boncheva M, Duschl C, Beck W, Jung G, Vogel H. Formation and characterization of lipopeptide layers at interfaces for the molecular recognition of antibodies. Langmuir. 12:1996;5636-5642 A complete study of antibody binding to a lipid-bound peptide segment of the picorna virus capsid protein VP1 at the air/water interface, after transfer to solid substrates, and in SUV's using CD, FTIR, SPM and FM is given.
    • (1996) Langmuir , vol.12 , pp. 5636-5642
    • Boncheva, M.1    Duschl, C.2    Beck, W.3    Jung, G.4    Vogel, H.5
  • 20
    • 0029565949 scopus 로고
    • Control of the specific adsorption of proteins onto gold surfaces with poly(L-lysine) monolayers
    • Prey BL, Jordan CE, Kornguth S, Corn RM. Control of the specific adsorption of proteins onto gold surfaces with poly(L-lysine) monolayers. Anal Chem. 67:1995;4452-4457.
    • (1995) Anal Chem , vol.67 , pp. 4452-4457
    • Prey, B.L.1    Jordan, C.E.2    Kornguth, S.3    Corn, R.M.4
  • 21
    • 17044451633 scopus 로고    scopus 로고
    • Novel biosensoric devices based on molecular protein hetero-multilayer films
    • K. Nagayama, Ebashi G. Japan Scientific Societies Press/Elsevier, Tokyo/Limerick, Comprehensive study describing new concepts for the supramolecular functionalization of surfaces and their practical application in biosensors technology. A cascade of biospecific interactions used for device preparation. Sample characterization with X-ray reflectometry and immunological techniques
    • Diederich A, Lösche M. Novel biosensoric devices based on molecular protein hetero-multilayer films. Nagayama K., Ebashi G. Protein array: an alternate biomolecular system. 34:1997;205-230 Japan Scientific Societies Press/Elsevier, Tokyo/Limerick, Comprehensive study describing new concepts for the supramolecular functionalization of surfaces and their practical application in biosensors technology. A cascade of biospecific interactions used for device preparation. Sample characterization with X-ray reflectometry and immunological techniques.
    • (1997) Protein Array: An Alternate Biomolecular System , vol.34 , pp. 205-230
    • Diederich, A.1    Lösche, M.2
  • 22
    • 13544259908 scopus 로고    scopus 로고
    • Langmuir films of Fc binding receptors engineered from protein A and protein G as a sublayer for immunoglobulin orientation
    • Dubrovsky T, Tronin A, Dubrovskaya S, Guryev O, Nicolini C. Langmuir films of Fc binding receptors engineered from protein A and protein G as a sublayer for immunoglobulin orientation. Thin Solid Films. 284/285:1996;698-702.
    • (1996) Thin Solid Films , vol.284-285 , pp. 698-702
    • Dubrovsky, T.1    Tronin, A.2    Dubrovskaya, S.3    Guryev, O.4    Nicolini, C.5
  • 23
    • 0342960827 scopus 로고    scopus 로고
    • Surface forces between protein A adsorbed mica surfaces
    • Comprehensive study of protein A interaction with charged surfaces
    • Hato M, Murata M, Yoshida T. Surface forces between protein A adsorbed mica surfaces. Colloid Surf A. 109:1996;345-361 Comprehensive study of protein A interaction with charged surfaces.
    • (1996) Colloid Surf a , vol.109 , pp. 345-361
    • Hato, M.1    Murata, M.2    Yoshida, T.3
  • 24
    • 0030126663 scopus 로고    scopus 로고
    • Immobilization of antibodies on a photoactive self-assembled monolayer on gold
    • System for photochemical protein immobilization. Complete structural and functional characterization by ellipsometry, XPS, SEM, AFM and immunological techniques. A general application to protein immobilization seems feasible.
    • Delamarche E, Sundarababu G, Biebuyck H, Michel B, Gerber C, Sigrist H, Wolf H, Ringsdorf H, Xanthopoulos N, Mathieu HJ. Immobilization of antibodies on a photoactive self-assembled monolayer on gold. Langmuir. 12:1996;1997-2006 System for photochemical protein immobilization. Complete structural and functional characterization by ellipsometry, XPS, SEM, AFM and immunological techniques. A general application to protein immobilization seems feasible.
    • (1996) Langmuir , vol.12 , pp. 1997-2006
    • Delamarche, E.1    Sundarababu, G.2    Biebuyck, H.3    Michel, B.4    Gerber, C.5    Sigrist, H.6    Wolf, H.7    Ringsdorf, H.8    Xanthopoulos, N.9    Mathieu, H.J.10
  • 25
    • 0030574149 scopus 로고    scopus 로고
    • Modified monolayer electrodes for electrochemical and piezoelectric analysis of substrate-receptor interactions - novel immunosensor electrodes
    • Blocking of electron transfer from redox enzymes to conducting substrates by insulating layers of Ig's. Detection by cyclic voltammetry.
    • Cohen Y, Levi S, Rubin S, Rubin S, Willner I. Modified monolayer electrodes for electrochemical and piezoelectric analysis of substrate-receptor interactions - novel immunosensor electrodes. J Electroanal Chem. 417:1996;65-75 Blocking of electron transfer from redox enzymes to conducting substrates by insulating layers of Ig's. Detection by cyclic voltammetry.
    • (1996) J Electroanal Chem , vol.417 , pp. 65-75
    • Cohen, Y.1    Levi, S.2    Rubin, S.3    Rubin, S.4    Willner, I.5
  • 26
    • 0030587065 scopus 로고    scopus 로고
    • Application of redox enzymes for probing the antigen-antibody association at monolayer interfaces - development of amperometric immunosensor electrodes
    • Blonder R, Katz E, Cohen Y, Itzhak N, Riklin A, Willner I. Application of redox enzymes for probing the antigen-antibody association at monolayer interfaces - development of amperometric immunosensor electrodes. Anal Chem. 68:1996;3151-3157.
    • (1996) Anal Chem , vol.68 , pp. 3151-3157
    • Blonder, R.1    Katz, E.2    Cohen, Y.3    Itzhak, N.4    Riklin, A.5    Willner, I.6
  • 28
    • 0030361808 scopus 로고    scopus 로고
    • Non-equilibrium electrosurface phenomena - A case of biological interest
    • Ortega Vinuesa JL, Hidalgo-Álvarez R. Non-equilibrium electrosurface phenomena - a case of biological interest. J Non-Equil Thermodyn. 21:1996;339-356.
    • (1996) J Non-Equil Thermodyn , vol.21 , pp. 339-356
    • Ortega Vinuesa, J.L.1    Hidalgo-Álvarez, R.2
  • 29
    • 0031103031 scopus 로고    scopus 로고
    • Influence of different parameters on a dual-fractal analysis for antigen-antibody binding kinetics for biosensor applications
    • Milum J, Sadana A. Influence of different parameters on a dual-fractal analysis for antigen-antibody binding kinetics for biosensor applications. J Colloid Interface Sci. 187:1997;128-138.
    • (1997) J Colloid Interface Sci , vol.187 , pp. 128-138
    • Milum, J.1    Sadana, A.2
  • 30
    • 0001209774 scopus 로고    scopus 로고
    • Scanning angle reflectometry study of the structure of antigen-antibody layers adsorbed on silica surfaces
    • Heinrich L, Mann EK, Voegel JC, Koper GJM, Schaaf P. Scanning angle reflectometry study of the structure of antigen-antibody layers adsorbed on silica surfaces. Langmuir. 12:1996;4857-4865.
    • (1996) Langmuir , vol.12 , pp. 4857-4865
    • Heinrich, L.1    Mann, E.K.2    Voegel, J.C.3    Koper, G.J.M.4    Schaaf, P.5
  • 31
    • 0030601081 scopus 로고    scopus 로고
    • Structure of protein layers during competitive adsorption
    • Lassen B, Malmsten M. Structure of protein layers during competitive adsorption. J Colloid Interface Sci. 180:1996;339-349.
    • (1996) J Colloid Interface Sci , vol.180 , pp. 339-349
    • Lassen, B.1    Malmsten, M.2
  • 32
    • 0031076421 scopus 로고    scopus 로고
    • Competitive protein adsorption at plasma polymer surfaces
    • Lassen B, Malmsten M. Competitive protein adsorption at plasma polymer surfaces. J Colloid Interface Sci. 186:1997;9-16.
    • (1997) J Colloid Interface Sci , vol.186 , pp. 9-16
    • Lassen, B.1    Malmsten, M.2
  • 33
    • 0030777594 scopus 로고    scopus 로고
    • SPR studies of the nonspecific adsorption kinetics of human IgG and BSA on gold surfaces modified by self-assembled monolayers (SAMs)
    • Silin V, Weetall H, Vanderah DJ. SPR studies of the nonspecific adsorption kinetics of human IgG and BSA on gold surfaces modified by self-assembled monolayers (SAMs). J Colloid Interface Sci. 185:1997;94-103.
    • (1997) J Colloid Interface Sci , vol.185 , pp. 94-103
    • Silin, V.1    Weetall, H.2    Vanderah, D.J.3
  • 34
    • 0030601466 scopus 로고    scopus 로고
    • AFM studies of protein adsorption 2. Characterization of immunoglobulin G adsorption by detergent washing
    • You HX, Lowe CR. AFM studies of protein adsorption 2. Characterization of immunoglobulin G adsorption by detergent washing. J Colloid Interface Sci. 182:1996;586-601.
    • (1996) J Colloid Interface Sci , vol.182 , pp. 586-601
    • You, H.X.1    Lowe, C.R.2
  • 35
    • 0000364502 scopus 로고    scopus 로고
    • Atomic force microscopic study of specific antigen/antibody binding
    • Browning-Kelley ME, Wadu-Mesthrige K, Hari V, Liu GY. Atomic force microscopic study of specific antigen/antibody binding. Langmuir. 13:1997;343-350.
    • (1997) Langmuir , vol.13 , pp. 343-350
    • Browning-Kelley, M.E.1    Wadu-Mesthrige, K.2    Hari, V.3    Liu, G.Y.4
  • 36
    • 0004474575 scopus 로고    scopus 로고
    • Mechanical properties of immunoglobulin G and albumin monolayers
    • Ahluwalia A, Stussi E, Domenici C. Mechanical properties of immunoglobulin G and albumin monolayers. Langmuir. 12:1996;416-422.
    • (1996) Langmuir , vol.12 , pp. 416-422
    • Ahluwalia, A.1    Stussi, E.2    Domenici, C.3
  • 38
    • 0343145679 scopus 로고    scopus 로고
    • Bacterial and archaeal S-layer proteins: Structure-function relationships and their biotechnological applications
    • Sleytr UB, Sára M. Bacterial and archaeal S-layer proteins: structure-function relationships and their biotechnological applications. TIBTECH. 15:1997;20-26.
    • (1997) TIBTECH , vol.15 , pp. 20-26
    • Sleytr, U.B.1    Sára, M.2
  • 39
    • 0031104094 scopus 로고    scopus 로고
    • Imaging of the early events of classical complement activation using antibodies and atomic force microscopy
    • An attempt is given on the determination of the sequence of events during platelet activation constituting an interesting approach that might be elaborate in future work.
    • Wälivaara B, Askendal A, Lundström I, Tengvall P. Imaging of the early events of classical complement activation using antibodies and atomic force microscopy. J Colloid Interface Sci. 187:1997;121-127 An attempt is given on the determination of the sequence of events during platelet activation constituting an interesting approach that might be elaborate in future work.
    • (1997) J Colloid Interface Sci , vol.187 , pp. 121-127
    • Wälivaara, B.1    Askendal, A.2    Lundström, I.3    Tengvall, P.4
  • 41
    • 5844374656 scopus 로고    scopus 로고
    • Surface-immobilized plasma proteins and platelet activation in the non-self-recognition of foreign materials
    • Nygren H, Tengvall P, Lundström I. Surface-immobilized plasma proteins and platelet activation in the non-self-recognition of foreign materials. J Vac Sci Technol A. 14:1996;669-673.
    • (1996) J Vac Sci Technol a , vol.14 , pp. 669-673
    • Nygren, H.1    Tengvall, P.2    Lundström, I.3
  • 42
    • 0000928735 scopus 로고    scopus 로고
    • Biomolecular recognition at phospholipid-covered polystyrene microspheres
    • Miceli Sicchierolli S, Carmona-Ribeiro AM. Biomolecular recognition at phospholipid-covered polystyrene microspheres. J Phys Chem. 100:1996;16771-16775.
    • (1996) J Phys Chem , vol.100 , pp. 16771-16775
    • Miceli Sicchierolli, S.1    Carmona-Ribeiro, A.M.2
  • 43
    • 0030189555 scopus 로고    scopus 로고
    • An electrochemical study of the interfacial and conformational behaviour of cytochrome c and other heme proteins
    • Hanrahan K-L, MacDonald SM, Roscoe SG. An electrochemical study of the interfacial and conformational behaviour of cytochrome c and other heme proteins. Electrochim Acta. 41:1996;2469-2479.
    • (1996) Electrochim Acta , vol.41 , pp. 2469-2479
    • Hanrahan K-L1    MacDonald, S.M.2    Roscoe, S.G.3
  • 44
    • 0000869507 scopus 로고
    • Characterization of mercaptoethylamine-modified gold electrode surface and analyses of direct electron transfer to putidaredoxin
    • Wong LS, Vilker VL, Yap WT, Reipa V. Characterization of mercaptoethylamine-modified gold electrode surface and analyses of direct electron transfer to putidaredoxin. Langmuir. 11:1995;4818-4822.
    • (1995) Langmuir , vol.11 , pp. 4818-4822
    • Wong, L.S.1    Vilker, V.L.2    Yap, W.T.3    Reipa, V.4
  • 45
    • 0001156827 scopus 로고    scopus 로고
    • Correlation of the structural decomposition and performance of pyridinethiolate surface modifiers at gold electrodes for the facilitation of cytochrome c heterogeneous electron-transfer reactions
    • Lamp BD, Hobara D, Porter MD, Niki K, Cotton TM. Correlation of the structural decomposition and performance of pyridinethiolate surface modifiers at gold electrodes for the facilitation of cytochrome c heterogeneous electron-transfer reactions. Langmuir. 13:1997;736-741.
    • (1997) Langmuir , vol.13 , pp. 736-741
    • Lamp, B.D.1    Hobara, D.2    Porter, M.D.3    Niki, K.4    Cotton, T.M.5
  • 46
    • 0001395529 scopus 로고
    • Electrochemical responses of cytochrome c on gold electrode modified with bis (4-pyridyl) disulfide/n-alkanethiol mixed monolayers
    • Sato Y, Mizutani F. Electrochemical responses of cytochrome c on gold electrode modified with bis (4-pyridyl) disulfide/n-alkanethiol mixed monolayers. Denki Kagaku. 63:1995;1173-1178.
    • (1995) Denki Kagaku , vol.63 , pp. 1173-1178
    • Sato, Y.1    Mizutani, F.2
  • 47
    • 0000382194 scopus 로고    scopus 로고
    • Electrical communication between components of self-assembled mixed monolayers
    • Fabrication of functional amperometric nanodevices by coadsorption of short linker molecules (aminoethanethiol) and long-chain electron shuttles (ferrocenylhexadecanethiol) into self-assembled monolayers that were subsequently incubated with glucose oxidase. Characterization entirely by CV leaves open questions whether the proposed mechanism, domain formation of the coadsorbed thiol species, is the only possible explanation of the optimal mxing ratio observed in the work.
    • Rubin S, Chow JT, Ferraris JP, Zawodzinski TA. Electrical communication between components of self-assembled mixed monolayers. Langmuir. 12:1996;363-370 Fabrication of functional amperometric nanodevices by coadsorption of short linker molecules (aminoethanethiol) and long-chain electron shuttles (ferrocenylhexadecanethiol) into self-assembled monolayers that were subsequently incubated with glucose oxidase. Characterization entirely by CV leaves open questions whether the proposed mechanism, domain formation of the coadsorbed thiol species, is the only possible explanation of the optimal mxing ratio observed in the work.
    • (1996) Langmuir , vol.12 , pp. 363-370
    • Rubin, S.1    Chow, J.T.2    Ferraris, J.P.3    Zawodzinski, T.A.4
  • 48
    • 0000829417 scopus 로고    scopus 로고
    • Contribution of lateral force and tapping mode microscopies to the study of mixed protein Langmuir-Blodgett films
    • Sommer F, Alexandre S, Dubreuil N, Lair D, Duc T-M, Valleton JM. Contribution of lateral force and tapping mode microscopies to the study of mixed protein Langmuir-Blodgett films. Langmuir. 13:1997;791-795.
    • (1997) Langmuir , vol.13 , pp. 791-795
    • Sommer, F.1    Alexandre, S.2    Dubreuil, N.3    Lair, D.4    Duc T-M5    Valleton, J.M.6
  • 49
    • 0030288934 scopus 로고    scopus 로고
    • Direct electron transfer to cytochrome c oxidase in self-assembled monolayers on gold electrodes
    • Li JH, Cheng GJ, Dong SJ. Direct electron transfer to cytochrome c oxidase in self-assembled monolayers on gold electrodes. J Electroanal Chem. 416:1996;97-104.
    • (1996) J Electroanal Chem , vol.416 , pp. 97-104
    • Li, J.H.1    Cheng, G.J.2    Dong, S.J.3
  • 50
    • 0030779460 scopus 로고    scopus 로고
    • Viologen-thiol self-assembled monolayers for immobilized horseradish peroxidase at gold electrode surface
    • Li JH, Yan JC, Deng Q, Cheng GJ, Dong SJ. Viologen-thiol self-assembled monolayers for immobilized horseradish peroxidase at gold electrode surface. Electrochim Acta. 42:1997;961-967.
    • (1997) Electrochim Acta , vol.42 , pp. 961-967
    • Li, J.H.1    Yan, J.C.2    Deng, Q.3    Cheng, G.J.4    Dong, S.J.5
  • 51
    • 0000913547 scopus 로고    scopus 로고
    • Nanoencapsulation of cytochrome c and horseradish peroxidase at the galleries of α-zirconium phosphate
    • Systematic investigation of protein (Cyt c and HRP) immobilization within the galleries of α-Zr phosphate or phosphonate under physiological conditions. Characterization of protein stability by UV/Vis and FTIR, of interlayer separation by XRD. Quantification of binding constants, redox and enzyme activity, and thermal stability of the proteins show differences between the protein species and the host systems.
    • Kumar CV, McLendon GL. Nanoencapsulation of cytochrome c and horseradish peroxidase at the galleries of α-zirconium phosphate. Chem Mater. 9:1997;863-870 Systematic investigation of protein (Cyt c and HRP) immobilization within the galleries of α-Zr phosphate or phosphonate under physiological conditions. Characterization of protein stability by UV/Vis and FTIR, of interlayer separation by XRD. Quantification of binding constants, redox and enzyme activity, and thermal stability of the proteins show differences between the protein species and the host systems.
    • (1997) Chem Mater , vol.9 , pp. 863-870
    • Kumar, C.V.1    McLendon, G.L.2
  • 52
    • 0001584340 scopus 로고    scopus 로고
    • Photo-active and electro-active protein films prepared by reconstitution with metalloporphyrins self-assembled on gold
    • 2+ in self-assembled monolayers on gold characterized with XPS, fluorescence spectroscopy and CV. The formation of surface-linked holo-myoglobin after incubation of the surfaces with apo-protein monitored spectroscopically and electrochemically.
    • 2+ in self-assembled monolayers on gold characterized with XPS, fluorescence spectroscopy and CV. The formation of surface-linked holo-myoglobin after incubation of the surfaces with apo-protein monitored spectroscopically and electrochemically.
    • (1996) J Mater Chem , vol.6 , pp. 369-374
    • Guo, L.H.1    McLendon, G.2    Razafitrimo, H.3    Gao, Y.L.4
  • 53
    • 0001514837 scopus 로고    scopus 로고
    • Surface-linked molecular monolayers of an engineered myoglobin - structure, stability, and function
    • Jiang M, Nölting B, Stayton PS, Sligar SG. Surface-linked molecular monolayers of an engineered myoglobin - structure, stability, and function. Langmuir. 12:1996;1278-1283.
    • (1996) Langmuir , vol.12 , pp. 1278-1283
    • Jiang, M.1    Nölting, B.2    Stayton, P.S.3    Sligar, S.G.4
  • 54
    • 0030212308 scopus 로고    scopus 로고
    • Perspectives for in situ scanning tunnel microscopic imaging of metalloproteins at HOPG surfaces
    • Andersen JET, Hallberg Jensen M, Möller P, Ulstrup J. Perspectives for in situ scanning tunnel microscopic imaging of metalloproteins at HOPG surfaces. Electrochim Acta. 41:1996;2005-2010.
    • (1996) Electrochim Acta , vol.41 , pp. 2005-2010
    • Andersen, J.E.T.1    Hallberg Jensen, M.2    Möller, P.3    Ulstrup, J.4
  • 55
    • 0001223404 scopus 로고    scopus 로고
    • Structural investigation of cytochrome f Langmuir-Blodgett films with scanning tunnelling microscopy - protein aggregation
    • Tazi A, Boussaad S, Derose JA, Leblanc RM. Structural investigation of cytochrome f Langmuir-Blodgett films with scanning tunnelling microscopy - protein aggregation. J Vac Sci Technol B. 14:1996;1476-1480.
    • (1996) J Vac Sci Technol B , vol.14 , pp. 1476-1480
    • Tazi, A.1    Boussaad, S.2    Derose, J.A.3    Leblanc, R.M.4
  • 56
    • 0030232292 scopus 로고    scopus 로고
    • Behaviour of firefly luciferase associated with Langmuir-Blodgett films
    • Marron-Brignone L, Morelis RM, Blum LJ, Coulet PR. Behaviour of firefly luciferase associated with Langmuir-Blodgett films. Thin Solid Films. 284/285:1996;784-788.
    • (1996) Thin Solid Films , vol.284-285 , pp. 784-788
    • Marron-Brignone, L.1    Morelis, R.M.2    Blum, L.J.3    Coulet, P.R.4
  • 57
    • 0011064563 scopus 로고    scopus 로고
    • Immobilization through adsorption of luciferase on Langmuir-Blodgett films - influence of the hydrophilicity or hydrophobicity of the surface on the enzyme kinetic behavior
    • Marron-Brignone L, Morelis RM, Coulet PR. Immobilization through adsorption of luciferase on Langmuir-Blodgett films - influence of the hydrophilicity or hydrophobicity of the surface on the enzyme kinetic behavior. Langmuir. 12:1996;5674-5680.
    • (1996) Langmuir , vol.12 , pp. 5674-5680
    • Marron-Brignone, L.1    Morelis, R.M.2    Coulet, P.R.3
  • 58
    • 0031034491 scopus 로고    scopus 로고
    • Functionalization of gold surfaces for specific and reversible attachment of a fused β-galactosidase and choline-receptor protein
    • Solid-phase functionalization of preformed self-assembled monolayers of dithioctic acid into H-bond stabilized mixed monolayers of hydroxy and ethoxy-spacered thiocholine terminated species. A previously characterized chimera protein is specifically bound and characterized with CV. An optimum in the binding of the enzyme is observed at 3% of the choline-functionalized species. Emphasis of the work described in the paper is on the solid-phase chemistry.
    • Madoz J, Kuznetzov BA, Medrano FJ, Garcia JL, Fernandez VM. Functionalization of gold surfaces for specific and reversible attachment of a fused β-galactosidase and choline-receptor protein. J Am Chem Soc. 119:1997;1043-1051 Solid-phase functionalization of preformed self-assembled monolayers of dithioctic acid into H-bond stabilized mixed monolayers of hydroxy and ethoxy-spacered thiocholine terminated species. A previously characterized chimera protein is specifically bound and characterized with CV. An optimum in the binding of the enzyme is observed at 3% of the choline-functionalized species. Emphasis of the work described in the paper is on the solid-phase chemistry.
    • (1997) J Am Chem Soc , vol.119 , pp. 1043-1051
    • Madoz, J.1    Kuznetzov, B.A.2    Medrano, F.J.3    Garcia, J.L.4    Fernandez, V.M.5
  • 59
    • 0029884516 scopus 로고    scopus 로고
    • Adsorption of lipase to silica and methylated silica surfaces
    • Wannerberger K, Arnebrant T. Adsorption of lipase to silica and methylated silica surfaces. J Colloid Interface Sci. 177:1996;316-324.
    • (1996) J Colloid Interface Sci , vol.177 , pp. 316-324
    • Wannerberger, K.1    Arnebrant, T.2
  • 60
    • 0000663924 scopus 로고    scopus 로고
    • Activity and adsorption of lipase from Humicola lanuginosa on surfaces with different wettabilities
    • Wannerberger K, Welin-Klintström S, Arnebrant T. Activity and adsorption of lipase from Humicola lanuginosa on surfaces with different wettabilities. Langmuir. 13:1997;784-790.
    • (1997) Langmuir , vol.13 , pp. 784-790
    • Wannerberger, K.1    Welin-Klintström, S.2    Arnebrant, T.3
  • 61
    • 0031553485 scopus 로고    scopus 로고
    • Bioactive nanostructure with glutamate dehydrogenase associated with LB films - protecting role of the enzyme molecules on the structural lipidic organization
    • Girard-Egrot AP, Mories RM, Coulet PR. Bioactive nanostructure with glutamate dehydrogenase associated with LB films - protecting role of the enzyme molecules on the structural lipidic organization. Thin Solid Films. 292:1997;282-289.
    • (1997) Thin Solid Films , vol.292 , pp. 282-289
    • Girard-Egrot, A.P.1    Mories, R.M.2    Coulet, P.R.3
  • 62
    • 0001400108 scopus 로고    scopus 로고
    • Molecular orientation in heme protein films adsorbed to hydrophilic and hydrophobic glass surfaces
    • Lee JE, Saavedra SS. Molecular orientation in heme protein films adsorbed to hydrophilic and hydrophobic glass surfaces. Langmuir. 12:1996;4025-4032.
    • (1996) Langmuir , vol.12 , pp. 4025-4032
    • Lee, J.E.1    Saavedra, S.S.2
  • 63
    • 1842327453 scopus 로고    scopus 로고
    • Molecular orientation distributions in protein films. 1. Cytochrome c adsorbed to substrates of variable surface chemistry
    • Molecular orientation of surface-bound heme groups quantified by a combination of dichroic adsorption spectroscopy (optical waveguide attenuated total reflection geometry) and dichroic emission spectroscopy (TIRF excitation) with Langmuir - Blodgett films of Zn tetrakis-octadecylpyridino-porphyrin as a gauge. Cyt c adsorbed to negatively charged arachidic acid Langmuir - Blodgett films shows a narrow orientation distribution, whereas adsorption to bare glass or to self-assembled monolayers of various composition produced samples of poorer orientational order.
    • Edmiston PL, Lee JE, Cheng S-S, Saavedra SS. Molecular orientation distributions in protein films. 1. Cytochrome c adsorbed to substrates of variable surface chemistry. J Am Chem Soc. 119:1997;560-570 Molecular orientation of surface-bound heme groups quantified by a combination of dichroic adsorption spectroscopy (optical waveguide attenuated total reflection geometry) and dichroic emission spectroscopy (TIRF excitation) with Langmuir - Blodgett films of Zn tetrakis-octadecylpyridino-porphyrin as a gauge. Cyt c adsorbed to negatively charged arachidic acid Langmuir - Blodgett films shows a narrow orientation distribution, whereas adsorption to bare glass or to self-assembled monolayers of various composition produced samples of poorer orientational order.
    • (1997) J Am Chem Soc , vol.119 , pp. 560-570
    • Edmiston, P.L.1    Lee, J.E.2    Cheng S-S3    Saavedra, S.S.4
  • 64
    • 1842365512 scopus 로고    scopus 로고
    • Molecular orientation distributions in protein films. 2. Site-directed immobilization of yeast cytochrome c on thiol-capped, self-assembled monolayers
    • Wood LL, Cheng S-S, Edmiston PL, Saavedra SS. Molecular orientation distributions in protein films. 2. Site-directed immobilization of yeast cytochrome c on thiol-capped, self-assembled monolayers. J Am Chem Soc. 119:1997;571-576.
    • (1997) J Am Chem Soc , vol.119 , pp. 571-576
    • Wood, L.L.1    Cheng S-S2    Edmiston, P.L.3    Saavedra, S.S.4
  • 65
    • 0000227258 scopus 로고    scopus 로고
    • Vectorially-oriented monolayers of cytochrome oxidase - fabrication and profile structures
    • Vectorial orientation of cytochrome oxidase at amine-terminate self-assembled monolayers estimated from a comparison of the electron density profile (from XRD) with EM data.
    • Edwards AM, Chupa JA, Strongin RM, Smith AB, Blasie JK, Bean JC. Vectorially-oriented monolayers of cytochrome oxidase - fabrication and profile structures. Langmuir. 13:1997;1634-1643 Vectorial orientation of cytochrome oxidase at amine-terminate self-assembled monolayers estimated from a comparison of the electron density profile (from XRD) with EM data.
    • (1997) Langmuir , vol.13 , pp. 1634-1643
    • Edwards, A.M.1    Chupa, J.A.2    Strongin, R.M.3    Smith, A.B.4    Blasie, J.K.5    Bean, J.C.6
  • 66
    • 0030231805 scopus 로고    scopus 로고
    • Determination of bacteriorhodopsin orientation in monolayers by infrared spectroscopy
    • Méthot M, Boucher F, Salesse C, Subirade M, Pézolet M. Determination of bacteriorhodopsin orientation in monolayers by infrared spectroscopy. Thin Solid Films. 284/285:1996;627-630.
    • (1996) Thin Solid Films , vol.284-285 , pp. 627-630
    • Méthot, M.1    Boucher, F.2    Salesse, C.3    Subirade, M.4    Pézolet, M.5
  • 67
    • 0030962247 scopus 로고    scopus 로고
    • Molecular handling of photosynthetic proteins for molecular assembly construction
    • K. Nagayama, Ebashi G. Tokyo/Limerick: Japan Scientific Societies Press/Elsevier. (Series Editor): Advances in Biophysics
    • Miyake J, Hara M. Molecular handling of photosynthetic proteins for molecular assembly construction. Nagayama K, Ebashi G. Protein array: an alternate biomolecular system. 34:1997;109-126 Japan Scientific Societies Press/Elsevier, Tokyo/Limerick. (Series Editor): Advances in Biophysics.
    • (1997) Protein Array: An Alternate Biomolecular System , vol.34 , pp. 109-126
    • Miyake, J.1    Hara, M.2
  • 68
    • 0030567279 scopus 로고    scopus 로고
    • Orientational and spectroscopic studies of Langmuir-Blodgett films of a photodynamic pigmental protein, allophycocyanin
    • He JA, Jiang L-J, Jiang L, Bi Z-C, Li J-R. Orientational and spectroscopic studies of Langmuir-Blodgett films of a photodynamic pigmental protein, allophycocyanin. Langmuir. 12:1996;1840-1845.
    • (1996) Langmuir , vol.12 , pp. 1840-1845
    • He, J.A.1    Jiang L-J2    Jiang, L.3    Bi Z-C4    Li J-R5
  • 69
    • 0031553507 scopus 로고    scopus 로고
    • Displacement current measurements of the dynamic charge transfer of photosynthetic reaction centers in monolayer LB films
    • Yasuda Y, Kawakami Y, Toyomata H. Displacement current measurements of the dynamic charge transfer of photosynthetic reaction centers in monolayer LB films. Thin Solid Films. 292:1997;189-191.
    • (1997) Thin Solid Films , vol.292 , pp. 189-191
    • Yasuda, Y.1    Kawakami, Y.2    Toyomata, H.3
  • 70
    • 8944238475 scopus 로고    scopus 로고
    • Experimental and theoretical study of the adsorption behavior and mass transfer kinetics of propranolol enantiomers on cellulase protein as the selector
    • Fornstedt T, Zhong GM, Bensetiti Z, Guiochon G. Experimental and theoretical study of the adsorption behavior and mass transfer kinetics of propranolol enantiomers on cellulase protein as the selector. Anal Chem. 68:1996;2370-2378.
    • (1996) Anal Chem , vol.68 , pp. 2370-2378
    • Fornstedt, T.1    Zhong, G.M.2    Bensetiti, Z.3    Guiochon, G.4
  • 71
    • 0030901324 scopus 로고    scopus 로고
    • Thermodynamic study of an unusual chiral separation - propranolol enantiomers on an immobilized cellulase
    • Fornstedt T, Sajonz P, Guiochon G. Thermodynamic study of an unusual chiral separation - propranolol enantiomers on an immobilized cellulase. J Am Chem Soc. 119:1997;1254-1264.
    • (1997) J Am Chem Soc , vol.119 , pp. 1254-1264
    • Fornstedt, T.1    Sajonz, P.2    Guiochon, G.3
  • 72
    • 0030588308 scopus 로고    scopus 로고
    • Control of protein adsorption in capillary electrophoresis via an irreversibly bound protein coating
    • Van Tassel PR, Miras D, Hagege A, Leroy M, Voegel JC, Schaaf P. Control of protein adsorption in capillary electrophoresis via an irreversibly bound protein coating. J Colloid Interface Sci. 183:1996;269-273.
    • (1996) J Colloid Interface Sci , vol.183 , pp. 269-273
    • Van Tassel, P.R.1    Miras, D.2    Hagege, A.3    Leroy, M.4    Voegel, J.C.5    Schaaf, P.6
  • 73
  • 74
    • 0001733592 scopus 로고    scopus 로고
    • Interaction between β-lactoglobulin and phospholipids at the air/water interface
    • Bos MA, Nylander T. Interaction between β-lactoglobulin and phospholipids at the air/water interface. Langmuir. 12:1996;2791-2797.
    • (1996) Langmuir , vol.12 , pp. 2791-2797
    • Bos, M.A.1    Nylander, T.2
  • 75
    • 0343371686 scopus 로고    scopus 로고
    • Competitive adsorption of β-lactoglobulin and β-casein with Span 80 at the oil-water interface and the effects on emulsion behaviour
    • Cornec M, Mackie AR, Wilde PJ, Clark DC. Competitive adsorption of β-lactoglobulin and β-casein with Span 80 at the oil-water interface and the effects on emulsion behaviour. Colloid Surf A. 114:1996;237-244.
    • (1996) Colloid Surf a , vol.114 , pp. 237-244
    • Cornec, M.1    Mackie, A.R.2    Wilde, P.J.3    Clark, D.C.4
  • 76
    • 0344307061 scopus 로고    scopus 로고
    • Adsorption of β-lactoglobulin A and B in relation to self-association: Effect of concentration and pH
    • Elofsson U, Paulsson MA, Arnebrandt T. Adsorption of β-lactoglobulin A and B in relation to self-association: effect of concentration and pH. Langmuir. 13:1997;1695-1700.
    • (1997) Langmuir , vol.13 , pp. 1695-1700
    • Elofsson, U.1    Paulsson, M.A.2    Arnebrandt, T.3
  • 78
    • 0343586501 scopus 로고    scopus 로고
    • Comparison of the dilational behaviour of adsorbed milk proteins at the air-water and oil-water interfaces
    • Williams A, Prins A. Comparison of the dilational behaviour of adsorbed milk proteins at the air-water and oil-water interfaces. Colloid Surf A. 114:1996;267-275.
    • (1996) Colloid Surf a , vol.114 , pp. 267-275
    • Williams, A.1    Prins, A.2
  • 79
    • 0029931084 scopus 로고    scopus 로고
    • Nisin adsorption and exchange with selected milk proteins at silanized silica surfaces
    • Lakamraju M, McGuire J, Daeschel M. Nisin adsorption and exchange with selected milk proteins at silanized silica surfaces. J Colloid Interface Sci. 178:1996;495-504.
    • (1996) J Colloid Interface Sci , vol.178 , pp. 495-504
    • Lakamraju, M.1    McGuire, J.2    Daeschel, M.3
  • 80
    • 0030170484 scopus 로고    scopus 로고
    • Dynamics of the adsorption of egg albumin at the silica-solution interface
    • Bajpai AK, Dengre R. Dynamics of the adsorption of egg albumin at the silica-solution interface. J Appl Polym Sci. 60:1996;2219-2225.
    • (1996) J Appl Polym Sci , vol.60 , pp. 2219-2225
    • Bajpai, A.K.1    Dengre, R.2
  • 81
    • 0030004626 scopus 로고    scopus 로고
    • The role of electrostatic forces in anomalous adsorption behavior of phosvitin at the air/water interface
    • Damodaran S, Xu SQ. The role of electrostatic forces in anomalous adsorption behavior of phosvitin at the air/water interface. J Colloid Interface Sci. 178:1996;426-435.
    • (1996) J Colloid Interface Sci , vol.178 , pp. 426-435
    • Damodaran, S.1    Xu, S.Q.2
  • 83
    • 0030248424 scopus 로고    scopus 로고
    • Adsorption kinetics of wild type and two synthetic stability mutants of T4 phage lysozyme at silanized silica surfaces
    • Evaluation of the binding kinetics of structurally stabilized and destabilized lysozyme mutants (lle3Cys, lle3Trp) in a model involving two different protein states. Less stable molecules adsorb preferentially in a state that interacts more strongly with the interface. Differences are more pronounced on hydrophilic than on hydrophobic interfaces.
    • Singla B, Krisdhasima V, McGuire J. Adsorption kinetics of wild type and two synthetic stability mutants of T4 phage lysozyme at silanized silica surfaces. J Colloid Interface Sci. 182:1996;292-296 Evaluation of the binding kinetics of structurally stabilized and destabilized lysozyme mutants (lle3Cys, lle3Trp) in a model involving two different protein states. Less stable molecules adsorb preferentially in a state that interacts more strongly with the interface. Differences are more pronounced on hydrophilic than on hydrophobic interfaces.
    • (1996) J Colloid Interface Sci , vol.182 , pp. 292-296
    • Singla, B.1    Krisdhasima, V.2    McGuire, J.3
  • 84
    • 0031568207 scopus 로고    scopus 로고
    • Surface tension kinetics of the wild type and four synthetic stability mutants of T4 phage lysozyme at the air-water interface
    • Wang J, McGuire J. Surface tension kinetics of the wild type and four synthetic stability mutants of T4 phage lysozyme at the air-water interface. J Colloid Interface Sci. 185:1997;317-323.
    • (1997) J Colloid Interface Sci , vol.185 , pp. 317-323
    • Wang, J.1    McGuire, J.2
  • 85
    • 0029994694 scopus 로고    scopus 로고
    • Kinetics of desorption of proteins from the surface of protein-coated alumina by various desorbing reagents
    • Sarkar D, Chattoraj DK. Kinetics of desorption of proteins from the surface of protein-coated alumina by various desorbing reagents. J Colloid Interface Sci. 178:1996;606-613.
    • (1996) J Colloid Interface Sci , vol.178 , pp. 606-613
    • Sarkar, D.1    Chattoraj, D.K.2
  • 86
    • 0000130781 scopus 로고    scopus 로고
    • Kinetics of the homogeneous exchange of lysozyme adsorbed on a titanium oxide surface
    • Bentaleb A, Ball V, Haikel Y, Voegel JC, Schaaf P. Kinetics of the homogeneous exchange of lysozyme adsorbed on a titanium oxide surface. Langmuir. 13:1997;729-735.
    • (1997) Langmuir , vol.13 , pp. 729-735
    • Bentaleb, A.1    Ball, V.2    Haikel, Y.3    Voegel, J.C.4    Schaaf, P.5
  • 87
    • 0001305024 scopus 로고    scopus 로고
    • Adsorption kinetics of nonradiolabeled lysozyme via surface pressure-area isotherms
    • Murray B.S. Adsorption kinetics of nonradiolabeled lysozyme via surface pressure-area isotherms. Langmuir. 13:1997;1850-1852.
    • (1997) Langmuir , vol.13 , pp. 1850-1852
    • Murray, B.S.1
  • 88
    • 0031553479 scopus 로고    scopus 로고
    • Kinetics of lysozyme adsorption at the air-buffer interface
    • Douillard R. Kinetics of lysozyme adsorption at the air-buffer interface. Thin Solid Films. 292:1997;169-172.
    • (1997) Thin Solid Films , vol.292 , pp. 169-172
    • Douillard, R.1
  • 89
    • 0030235627 scopus 로고    scopus 로고
    • Surface activity of the insect defensin A and its interactions with lipids in mixed monolayers
    • Maget-Dana R, Hetru C, Ptak M. Surface activity of the insect defensin A and its interactions with lipids in mixed monolayers. Thin Solid Films. 284/285:1996;841-844.
    • (1996) Thin Solid Films , vol.284-285 , pp. 841-844
    • Maget-Dana, R.1    Hetru, C.2    Ptak, M.3
  • 91
    • 0030590889 scopus 로고    scopus 로고
    • Langmuir - Blodgett monolayers and multilayers of gramicidin A and lipids as membrane-mimetic models
    • Vila N, Puggelli M, Gabrielli G. Langmuir - Blodgett monolayers and multilayers of gramicidin A and lipids as membrane-mimetic models. Colloid Surf A. 119:1996;95-104.
    • (1996) Colloid Surf a , vol.119 , pp. 95-104
    • Vila, N.1    Puggelli, M.2    Gabrielli, G.3
  • 92
    • 0011319665 scopus 로고    scopus 로고
    • Two-dimensional molecular assembling of calmodulin-melittin at the air-water interface
    • Damrongchai N, Kobatake E, Ikariyama Y, Aizawa M. Two-dimensional molecular assembling of calmodulin-melittin at the air-water interface. Langmuir. 12:1996;1321-1325.
    • (1996) Langmuir , vol.12 , pp. 1321-1325
    • Damrongchai, N.1    Kobatake, E.2    Ikariyama, Y.3    Aizawa, M.4
  • 93
    • 0030077272 scopus 로고    scopus 로고
    • A self-assembled monolayer for the binding and study of histidine tagged proteins by surface plasmon resonance
    • The high specificity of Ni-dependent binding of his-tagged proteins to nitriloacetic acid terminated self-assembled monolayers is demonstrated using surface plasmon resonance. Binding quantitatively reversible with imidazole. Interaction of immobilized proteins with secondary ligands from the fluid adphase is more efficient than with his-tagged proteins bound to carboxy-dextrane layers. Very elegant and flexible approach, similar to Kubalek (et al. J Struct Biol 1994, 113: 117.)
    • Sigal GB, Bamdad C, Barberies A, Strominger J, Whitesides GM. A self-assembled monolayer for the binding and study of histidine tagged proteins by surface plasmon resonance. Anal Chem. 68:1996;490-497 The high specificity of Ni-dependent binding of his-tagged proteins to nitriloacetic acid terminated self-assembled monolayers is demonstrated using surface plasmon resonance. Binding quantitatively reversible with imidazole. Interaction of immobilized proteins with secondary ligands from the fluid adphase is more efficient than with his-tagged proteins bound to carboxy-dextrane layers. Very elegant and flexible approach, similar to Kubalek (et al. J Struct Biol 1994, 113: 117.).
    • (1996) Anal Chem , vol.68 , pp. 490-497
    • Sigal, G.B.1    Bamdad, C.2    Barberies, A.3    Strominger, J.4    Whitesides, G.M.5
  • 94
    • 0030901962 scopus 로고    scopus 로고
    • A metal-chelating lipid for 2D protein crystallization via coordination of surface histidines
    • A metal-chelating lipid is constructed for the binding and crystallization of water soluble proteins. Whereas in earlier work, functionalized lipids had to be synthesized for each application, this approach derives its attractiveness from its flexibility for the immobilization of various proteins with surface-exposed histidines.
    • Pack DW, Chen GH, Maloney KM, Chen C-T, Arnold FH. A metal-chelating lipid for 2D protein crystallization via coordination of surface histidines. J Am Chem Soc. 119:1997;2479-2487 A metal-chelating lipid is constructed for the binding and crystallization of water soluble proteins. Whereas in earlier work, functionalized lipids had to be synthesized for each application, this approach derives its attractiveness from its flexibility for the immobilization of various proteins with surface-exposed histidines.
    • (1997) J Am Chem Soc , vol.119 , pp. 2479-2487
    • Pack, D.W.1    Chen, G.H.2    Maloney, K.M.3    Chen C-T4    Arnold, F.H.5
  • 95
    • 0030054542 scopus 로고    scopus 로고
    • ATP-lipids - protein anchor and energy source in two dimensions
    • Synthesis of AMP- and ATP-functionalized lipids with various spacer lengths between the aliphatic chains and the ATP function and with hydrolyzable and nonhydrolyzable triphosphates. As a first application of such compounds, the surface-dependent polymerization of actin is shown. 2D crystallization of ATP-binding proteins and 2D reservoirs of ATP for ATP-dependent reactions discussed as further applications.
    • Schmitt L, Tampé R. ATP-lipids - protein anchor and energy source in two dimensions. J Am Chem Soc. 118:1996;5532-5543 Synthesis of AMP- and ATP-functionalized lipids with various spacer lengths between the aliphatic chains and the ATP function and with hydrolyzable and nonhydrolyzable triphosphates. As a first application of such compounds, the surface-dependent polymerization of actin is shown. 2D crystallization of ATP-binding proteins and 2D reservoirs of ATP for ATP-dependent reactions discussed as further applications.
    • (1996) J Am Chem Soc , vol.118 , pp. 5532-5543
    • Schmitt, L.1    Tampé, R.2
  • 96
    • 0030043338 scopus 로고    scopus 로고
    • Specific protein docking to chelator lipid-monolayers monitored by FT-IR spectroscopy at the air-water interface
    • Int Ed
    • Schmitt L, Bohanon TM, Denzinger TM, Ringsdorf H, Tampé R. Specific protein docking to chelator lipid-monolayers monitored by FT-IR spectroscopy at the air-water interface. Int Ed Angew Chem. 35:1996;317-320.
    • (1996) Angew Chem , vol.35 , pp. 317-320
    • Schmitt, L.1    Bohanon, T.M.2    Denzinger, T.M.3    Ringsdorf, H.4    Tampé, R.5
  • 97
    • 0030069974 scopus 로고    scopus 로고
    • Functional immobilization of a DNA-binding protein at a membrane interface via histidine tag and synthetic chelator lipids
    • Dietrich C, Boscheinen O, Scharf K-D, Schmitt L, Tampé R. Functional immobilization of a DNA-binding protein at a membrane interface via histidine tag and synthetic chelator lipids. Biochemistry. 35:1996;1100-1105.
    • (1996) Biochemistry , vol.35 , pp. 1100-1105
    • Dietrich, C.1    Boscheinen, O.2    Scharf K-D3    Schmitt, L.4    Tampé, R.5
  • 98
    • 0029185755 scopus 로고
    • Biospecific adsorption of carbonic anhydrase to self-assembled monolayers of alkanethiolates that present benzenesulfonamide groups on gold
    • Mrksich M, Grunwell JR, Whitesides GM. Biospecific adsorption of carbonic anhydrase to self-assembled monolayers of alkanethiolates that present benzenesulfonamide groups on gold. J Am Chem Soc. 117:1995;12009-12010.
    • (1995) J Am Chem Soc , vol.117 , pp. 12009-12010
    • Mrksich, M.1    Grunwell, J.R.2    Whitesides, G.M.3
  • 100
    • 0030262665 scopus 로고    scopus 로고
    • Supramolecular assembly containing hydrophobic α-helical oligopeptide molecules
    • Imanishi Y, Kimura S. Supramolecular assembly containing hydrophobic α-helical oligopeptide molecules. Polymers. 37:1996;4929-4935.
    • (1996) Polymers , vol.37 , pp. 4929-4935
    • Imanishi, Y.1    Kimura, S.2
  • 101
    • 0002265616 scopus 로고    scopus 로고
    • Design and synthesis of flavin-conjugated peptides and assembly on a gold electrode
    • Sakamoto S, Aoyagi H, Nakashima N, Mihara H. Design and synthesis of flavin-conjugated peptides and assembly on a gold electrode. J Chem Soc Perkin Trans II. 11:1996;2319-2326.
    • (1996) J Chem Soc Perkin Trans II , vol.11 , pp. 2319-2326
    • Sakamoto, S.1    Aoyagi, H.2    Nakashima, N.3    Mihara, H.4
  • 102
    • 0029804670 scopus 로고    scopus 로고
    • Film architecture in biomolecular assemblies - effect of linker on the orientation of genetically engineered surface-bound proteins
    • Firestone MA, Shank ML, Sligar SG, Bohn PW. Film architecture in biomolecular assemblies - effect of linker on the orientation of genetically engineered surface-bound proteins. J Am Chem Soc. 118:1996;9033-9041.
    • (1996) J Am Chem Soc , vol.118 , pp. 9033-9041
    • Firestone, M.A.1    Shank, M.L.2    Sligar, S.G.3    Bohn, P.W.4
  • 103
    • 0029387775 scopus 로고
    • The specific adsorption of streptavidin to a tetrabiotinylated porphyrin monolayer at the air-water interface
    • Fukushima H, Taylor DM, Morgan H, Ringsdorf H, Rump E. The specific adsorption of streptavidin to a tetrabiotinylated porphyrin monolayer at the air-water interface. Thin Solid Films. 266:1995;289-291.
    • (1995) Thin Solid Films , vol.266 , pp. 289-291
    • Fukushima, H.1    Taylor, D.M.2    Morgan, H.3    Ringsdorf, H.4    Rump, E.5
  • 104
    • 0001638018 scopus 로고    scopus 로고
    • Two-dimensional crystallization of streptavidin studied by quantitative Brewster angle microscopy
    • For streptavidin specifically bound to biotinylated lipids at the air/water interface it is shown that crystallization requires a critical protein density at the interface that amounts to -75% of the density in the crystal. Compression of the mixed crystalline-amorphous film results in a protein density of the amorphous areas larger than that of the 2D crystal. However, crystallization was not induced in these dense amorphous regions.
    • Frey W, Schief WR Jr, Vogel V. Two-dimensional crystallization of streptavidin studied by quantitative Brewster angle microscopy. Langmuir. 12:1996;1312-1320 For streptavidin specifically bound to biotinylated lipids at the air/water interface it is shown that crystallization requires a critical protein density at the interface that amounts to -75% of the density in the crystal. Compression of the mixed crystalline-amorphous film results in a protein density of the amorphous areas larger than that of the 2D crystal. However, crystallization was not induced in these dense amorphous regions.
    • (1996) Langmuir , vol.12 , pp. 1312-1320
    • Frey, W.1    Schief W.R., Jr.2    Vogel, V.3
  • 106
    • 0001612509 scopus 로고    scopus 로고
    • Phase-separated two-component self-assembled organosilane monolayers and their use in selective adsorption of a protein
    • Trichlorosilane monolayers spread at the air/water interface form phase-separated structures that may be transferred to mica. Whereas the condensed phase is preserved upon transfer the dilute phase is not, which creates empty spaces on the substrate that may be subsequently filled in (with other molecular species) by conventional self-assembly. The well-defined microscopic chemical topology is a powerful tool to study the basic principles of protein adsorption.
    • Fang J, Knobler CM. Phase-separated two-component self-assembled organosilane monolayers and their use in selective adsorption of a protein. Langmuir. 12:1996;1368-1374 Trichlorosilane monolayers spread at the air/water interface form phase-separated structures that may be transferred to mica. Whereas the condensed phase is preserved upon transfer the dilute phase is not, which creates empty spaces on the substrate that may be subsequently filled in (with other molecular species) by conventional self-assembly. The well-defined microscopic chemical topology is a powerful tool to study the basic principles of protein adsorption.
    • (1996) Langmuir , vol.12 , pp. 1368-1374
    • Fang, J.1    Knobler, C.M.2
  • 107
    • 0000400537 scopus 로고    scopus 로고
    • Scanning force microscopic studies of surface structure and protein adsorption behavior of organosilane monolayers
    • Takahara A, Kojio K, Ge SR, Kajiyama T. Scanning force microscopic studies of surface structure and protein adsorption behavior of organosilane monolayers. J Vac Sci Technol A. 14:1996;1747-1754.
    • (1996) J Vac Sci Technol a , vol.14 , pp. 1747-1754
    • Takahara, A.1    Kojio, K.2    Ge, S.R.3    Kajiyama, T.4
  • 108
    • 0343831901 scopus 로고    scopus 로고
    • Two-dimensional self-assembly of colloids in thin liquid films
    • Nagayama K. Two-dimensional self-assembly of colloids in thin liquid films. Colloid Surf A. 109:1996;363-374.
    • (1996) Colloid Surf a , vol.109 , pp. 363-374
    • Nagayama, K.1
  • 109
    • 0030926757 scopus 로고    scopus 로고
    • Assembly process of 2D protein arrays in wetting films
    • K. Nagayama, Ebashi G. Tokyo/Limerick: Japan Scientific Societies Press/Elsevier. (Series Editor) Advances in Biophysics
    • Adachi E, Nagayama K. Assembly process of 2D protein arrays in wetting films. Nagayama K, Ebashi G. Protein array: An alternate biomolecular system. 34:1997;81-92 Japan Scientific Societies Press/Elsevier, Tokyo/Limerick. (Series Editor) Advances in Biophysics.
    • (1997) Protein Array: An Alternate Biomolecular System , vol.34 , pp. 81-92
    • Adachi, E.1    Nagayama, K.2
  • 110
    • 0030567292 scopus 로고    scopus 로고
    • Formation of holoferritin hexagonal arrays in secondary films due to alder-type transition
    • Adachi E, Nagayama K. Formation of holoferritin hexagonal arrays in secondary films due to alder-type transition. Langmuir. 12:1996;1836-1839.
    • (1996) Langmuir , vol.12 , pp. 1836-1839
    • Adachi, E.1    Nagayama, K.2
  • 111
    • 0004317222 scopus 로고    scopus 로고
    • Stabilization of a fragile two-dimensional protein crystal at the water-air interface - The square lattice of apoferritin
    • Scheybani T, Yoshimura H, Baumeister W, Nagayama K. Stabilization of a fragile two-dimensional protein crystal at the water-air interface - The square lattice of apoferritin. Langmuir. 12:1996;431-435.
    • (1996) Langmuir , vol.12 , pp. 431-435
    • Scheybani, T.1    Yoshimura, H.2    Baumeister, W.3    Nagayama, K.4
  • 112
    • 0030230819 scopus 로고    scopus 로고
    • Two-dimensional crystallization of ferritin molecules at the air-water interface
    • Yase K, Udaka T. Two-dimensional crystallization of ferritin molecules at the air-water interface. J Cryst Growth. 166:1996;946-951.
    • (1996) J Cryst Growth , vol.166 , pp. 946-951
    • Yase, K.1    Udaka, T.2
  • 113
    • 0031011399 scopus 로고    scopus 로고
    • Two-dimensional crystals of apoferritin
    • K. Nagayama, Ebashi G. Tokyo/Limerick: Japan Scientific Societies Press/Elsevier. (Series Editor): Advances in Biophysics
    • Yoshimura H. Two-dimensional crystals of apoferritin. Nagayama K, Ebashi G. Protein array: an alternate biomolecular system. 34:1997;93-107 Japan Scientific Societies Press/Elsevier, Tokyo/Limerick. (Series Editor): Advances in Biophysics.
    • (1997) Protein Array: An Alternate Biomolecular System , vol.34 , pp. 93-107
    • Yoshimura, H.1
  • 114
    • 0030565921 scopus 로고    scopus 로고
    • 2D-crystallization of Rhodococcus 20s proteasome at the liquid-liquid interface
    • Aoyama K. 2D-crystallization of Rhodococcus 20s proteasome at the liquid-liquid interface. J Cryst Growth. 168:1996;198-203.
    • (1996) J Cryst Growth , vol.168 , pp. 198-203
    • Aoyama, K.1
  • 115
    • 0030392065 scopus 로고    scopus 로고
    • Trigonal crystal structure of Bombyx mori silk incorporating a threefold helical chain conformation found at the air-water interface
    • Valluzzi R, Gido SP, Zhang WP, Muller WS, Kaplan DL. Trigonal crystal structure of Bombyx mori silk incorporating a threefold helical chain conformation found at the air-water interface. Macromolecules. 29:1996;8606-8614.
    • (1996) Macromolecules , vol.29 , pp. 8606-8614
    • Valluzzi, R.1    Gido, S.P.2    Zhang, W.P.3    Muller, W.S.4    Kaplan, D.L.5
  • 116
    • 0343580439 scopus 로고    scopus 로고
    • Functionalized lipid tubules as tools for helical crystallization of proteins
    • Ringler P, Müller W, Ringsdorf H, Brisson A. Functionalized lipid tubules as tools for helical crystallization of proteins. Chem Eur J. 3:1997;620-625.
    • (1997) Chem Eur J , vol.3 , pp. 620-625
    • Ringler, P.1    Müller, W.2    Ringsdorf, H.3    Brisson, A.4
  • 117
    • 0030397047 scopus 로고    scopus 로고
    • Imaging two-dimensional crystals of catalase by atomic force microscopy
    • Ohnishi S, Hara M, Furuno T, Sasabe H. Imaging two-dimensional crystals of catalase by atomic force microscopy. Jpn J Appl Phys. 35:1996;6233-6238.
    • (1996) Jpn J Appl Phys , vol.35 , pp. 6233-6238
    • Ohnishi, S.1    Hara, M.2    Furuno, T.3    Sasabe, H.4
  • 118
    • 0040324124 scopus 로고    scopus 로고
    • Hydrogen bonding molecules and their effect on scanning tunneling microscope image contrast of covalently immobilized protein molecules
    • Parker MC, Davies MC, Tendler SJB. Hydrogen bonding molecules and their effect on scanning tunneling microscope image contrast of covalently immobilized protein molecules. J Vac Sci Technol B. 14:1996;1432-1437.
    • (1996) J Vac Sci Technol B , vol.14 , pp. 1432-1437
    • Parker, M.C.1    Davies, M.C.2    Tendler, S.J.B.3
  • 119
    • 0343985339 scopus 로고    scopus 로고
    • Specific adsorption of flagellar FliF protein ring on mica surfaces as studied by atomic force microscopy and FT-IR spectroscopy
    • Kurihara K, Mizukami M, Suzuki K, Oosawa K. Specific adsorption of flagellar FliF protein ring on mica surfaces as studied by atomic force microscopy and FT-IR spectroscopy. Colloid Surf A. 109:1996;375-384.
    • (1996) Colloid Surf a , vol.109 , pp. 375-384
    • Kurihara, K.1    Mizukami, M.2    Suzuki, K.3    Oosawa, K.4
  • 120
    • 0031000467 scopus 로고    scopus 로고
    • The influence of protein and interfacial structure on the self-assembly of oriented protein arrays
    • K. Nagayama, Ebashi G. Japan Scientific Societies Press/Elsevier, Tokyo/Limerick, Biospecific recognition events characterized in the SFA. The impact of protein structure and electrostatic forces on the self-assembly of supramolecular structures involving proteins
    • Leckband DE. The influence of protein and interfacial structure on the self-assembly of oriented protein arrays. Nagayama K, Ebashi G. Protein array: an alternate biomolecular system. 34:1997;173-190 Japan Scientific Societies Press/Elsevier, Tokyo/Limerick, Biospecific recognition events characterized in the SFA. The impact of protein structure and electrostatic forces on the self-assembly of supramolecular structures involving proteins.
    • (1997) Protein Array: An Alternate Biomolecular System , vol.34 , pp. 173-190
    • Leckband, D.E.1
  • 121
    • 0030960136 scopus 로고    scopus 로고
    • Advances in S-layer nanotestrchnology and biomimetics
    • K. Nagayama, Ebashi G. Tokyo/Limerick: Japan Scientific Societies Press/Elsevier. (Series Editor): Advances in Biophysics
    • Sleytr UB, Pum D, Sára M. Advances in S-layer nanotestrchnology and biomimetics. Nagayama K, Ebashi G. Protein array: an alternate biomolecular system. 34:1997;71-81 Japan Scientific Societies Press/Elsevier, Tokyo/Limerick. (Series Editor): Advances in Biophysics.
    • (1997) Protein Array: An Alternate Biomolecular System , vol.34 , pp. 71-81
    • Sleytr, U.B.1    Pum, D.2    Sára, M.3
  • 122
    • 0000254578 scopus 로고    scopus 로고
    • Dynamic thin laminar flow method for making protein monolayers
    • Picard G, Nevernov I, Alliata D, Pazdernik L. Dynamic thin laminar flow method for making protein monolayers. Langmuir. 13:1997;264-276.
    • (1997) Langmuir , vol.13 , pp. 264-276
    • Picard, G.1    Nevernov, I.2    Alliata, D.3    Pazdernik, L.4
  • 123
    • 0030588137 scopus 로고    scopus 로고
    • Effect of diffusional losses on the formation of monolayers of soluble proteins at air/water interfaces with trumits method
    • Cho DC, Franses El, Narsimhan G. Effect of diffusional losses on the formation of monolayers of soluble proteins at air/water interfaces with trumits method. Colloid Surf A. 117:1996;45-54.
    • (1996) Colloid Surf a , vol.117 , pp. 45-54
    • Cho, D.C.1    Franses El2    Narsimhan, G.3
  • 124
    • 21844501285 scopus 로고
    • Reconstitution of membrane proteins into lipid monolayer: Two-step transfer technique: From cell to liposome, from liposome to lipid monolayer
    • Glück G, Okumura Y, Sunamoto J. Reconstitution of membrane proteins into lipid monolayer: Two-step transfer technique: from cell to liposome, from liposome to lipid monolayer. Chem Lett. 1995;1031-1032.
    • (1995) Chem Lett , pp. 1031-1032
    • Glück, G.1    Okumura, Y.2    Sunamoto, J.3
  • 125
    • 0030233180 scopus 로고    scopus 로고
    • Interaction of two lipid binding proteins with membrane lipids: Comparative study using the monolayer technique and IR spectroscopy
    • Subirade M, Marion D, Pézolet M. Interaction of two lipid binding proteins with membrane lipids: comparative study using the monolayer technique and IR spectroscopy. Thin Solid Films. 284/285:1996;326-329.
    • (1996) Thin Solid Films , vol.284-285 , pp. 326-329
    • Subirade, M.1    Marion, D.2    Pézolet, M.3
  • 126
    • 0030233747 scopus 로고    scopus 로고
    • Specific interaction of rabbit C-reactive protein with phospholipid membranes
    • Caide X, Liu Z, Gao Q-F, Zhou Q-Z, Sui S-F. Specific interaction of rabbit C-reactive protein with phospholipid membranes. Thin Solid Films. 284/285:1996;793-796.
    • (1996) Thin Solid Films , vol.284-285 , pp. 793-796
    • Caide, X.1    Liu, Z.2    Gao Q-F3    Zhou Q-Z4    Sui S-F5
  • 127
    • 0029844584 scopus 로고    scopus 로고
    • Synthesis, lipophilic derivatization and interaction with liposomes of HAV-VP3 (102-121) sequence by using spectroscopic techniques
    • Garcia M, Pujol M, Reig F, Alsina MA, Haro I. Synthesis, lipophilic derivatization and interaction with liposomes of HAV-VP3 (102-121) sequence by using spectroscopic techniques. Analyst. 121:1996;1583-1588.
    • (1996) Analyst , vol.121 , pp. 1583-1588
    • Garcia, M.1    Pujol, M.2    Reig, F.3    Alsina, M.A.4    Haro, I.5
  • 128
    • 0029891834 scopus 로고    scopus 로고
    • Reciprocal influence between the protein and lipid components of a lipid-protein membrane model
    • S-proteins are shown to specifically nucleate crystal growth at solid lipid domains in a phase-separated surface monolayer. Vice versa, protein crystallization increases the order of alkane chains of the lipid. As the protein is believed to attach externally to the lipid membrane, a coupling between the chains and head groups is postulated to transfer information on the chain order to the space external to the membrane.
    • Diederich A, Sponer C, Pum D, Sleytr UB, Lösche M. Reciprocal influence between the protein and lipid components of a lipid-protein membrane model. Colloid Surf B. 6:1996;335-346 S-proteins are shown to specifically nucleate crystal growth at solid lipid domains in a phase-separated surface monolayer. Vice versa, protein crystallization increases the order of alkane chains of the lipid. As the protein is believed to attach externally to the lipid membrane, a coupling between the chains and head groups is postulated to transfer information on the chain order to the space external to the membrane.
    • (1996) Colloid Surf B , vol.6 , pp. 335-346
    • Diederich, A.1    Sponer, C.2    Pum, D.3    Sleytr, U.B.4    Lösche, M.5
  • 129
    • 0031194869 scopus 로고    scopus 로고
    • S-layer stabilized solid supported lipid bilayers
    • Wetzer B, Pum D, Sleytr UB. S-layer stabilized solid supported lipid bilayers. J Struct Biol. 119:1997;123-128.
    • (1997) J Struct Biol , vol.119 , pp. 123-128
    • Wetzer, B.1    Pum, D.2    Sleytr, U.B.3
  • 130
    • 17044446782 scopus 로고    scopus 로고
    • Assessment of pulmonary surfactant function using a captive-bubble surfactometer
    • Herold R, Bünger H, Pison U. Assessment of pulmonary surfactant function using a captive-bubble surfactometer. Colloid Surf A. 114:1996;211-219.
    • (1996) Colloid Surf a , vol.114 , pp. 211-219
    • Herold, R.1    Bünger, H.2    Pison, U.3
  • 131
    • 0029789206 scopus 로고    scopus 로고
    • Phase and morphology changes in lipid monolayers induced by SP-B protein and its amino-terminal peptide
    • Lipp MM, Lee KYC, Zasadzinski JA, Waring AJ. Phase and morphology changes in lipid monolayers induced by SP-B protein and its amino-terminal peptide. Science. 273:1996;1196-1199.
    • (1996) Science , vol.273 , pp. 1196-1199
    • Lipp, M.M.1    Lee, K.Y.C.2    Zasadzinski, J.A.3    Waring, A.J.4
  • 132
    • 0030234524 scopus 로고    scopus 로고
    • Effect of water activity on unfolding of adsorbed protein at the interface
    • Shibata A, Iizuka Y, Ueno S, Yamashita T. Effect of water activity on unfolding of adsorbed protein at the interface. Thin Solid Films. 284/285:1996;549-551.
    • (1996) Thin Solid Films , vol.284-285 , pp. 549-551
    • Shibata, A.1    Iizuka, Y.2    Ueno, S.3    Yamashita, T.4
  • 133
    • 0030156588 scopus 로고    scopus 로고
    • Role of protein unfolding in monolayer formation of air-water interface
    • Tronin A, Dubrovsky T, Dubrovskaya S, Radicchi G, Nicolini C. Role of protein unfolding in monolayer formation of air-water interface. Langmuir. 12:1996;3272-3275.
    • (1996) Langmuir , vol.12 , pp. 3272-3275
    • Tronin, A.1    Dubrovsky, T.2    Dubrovskaya, S.3    Radicchi, G.4    Nicolini, C.5
  • 134
    • 0030529816 scopus 로고    scopus 로고
    • Vertical sectioning of molecular assemblies at air water interface using laser scanning confocal fluorescence microscopy
    • Glück G, Ringsdorf H, Okumura Y, Sunamoto J. Vertical sectioning of molecular assemblies at air water interface using laser scanning confocal fluorescence microscopy. Chem Lett. 1996;209-210.
    • (1996) Chem Lett , pp. 209-210
    • Glück, G.1    Ringsdorf, H.2    Okumura, Y.3    Sunamoto, J.4
  • 135
    • 0001365992 scopus 로고    scopus 로고
    • Spontaneous reconfiguration of adsorbed lysozyme layers observed by total internal reflection fluorescence with a pH-sensitive fluorophore
    • pH-sensitivity of fluoresceine isothiocyanate utilized to fine-tune the emission from surface-bound labeled protein, resulting in an effective decrease of the characteristic length scale of surface sensitivity from optical wavelengths to the Debye length. This enables the characterization of protein reorganization upon crowding at the interface in molecular terms.
    • Robeson JL, Tilton RD. Spontaneous reconfiguration of adsorbed lysozyme layers observed by total internal reflection fluorescence with a pH-sensitive fluorophore. Langmuir. 12:1996;6104-6113 pH-sensitivity of fluoresceine isothiocyanate utilized to fine-tune the emission from surface-bound labeled protein, resulting in an effective decrease of the characteristic length scale of surface sensitivity from optical wavelengths to the Debye length. This enables the characterization of protein reorganization upon crowding at the interface in molecular terms.
    • (1996) Langmuir , vol.12 , pp. 6104-6113
    • Robeson, J.L.1    Tilton, R.D.2
  • 137
    • 0030181284 scopus 로고    scopus 로고
    • Broad-band attenuated total reflection spectroscopy of a hydrated protein film on a single mode planar waveguide
    • Mendes SB, Li L-F, Burke JJ, Lee JE, Dunphy DR, Saavedra SS. Broad-band attenuated total reflection spectroscopy of a hydrated protein film on a single mode planar waveguide. Langmuir. 12:1996;3374-3376.
    • (1996) Langmuir , vol.12 , pp. 3374-3376
    • Mendes, S.B.1    Li L-F2    Burke, J.J.3    Lee, J.E.4    Dunphy, D.R.5    Saavedra, S.S.6
  • 138
    • 0000445450 scopus 로고    scopus 로고
    • Waveguide raman spectroscopy of thin polymer layers and monolayers of biomolecules using high refractive index waveguides
    • Sake Kanger J, Otto C, Slotboom M, Greve J. Waveguide raman spectroscopy of thin polymer layers and monolayers of biomolecules using high refractive index waveguides. J Phys Chem. 100:1996;3288-3282.
    • (1996) J Phys Chem , vol.100 , pp. 3288-3282
    • Sake Kanger, J.1    Otto, C.2    Slotboom, M.3    Greve, J.4
  • 139
    • 1542467523 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging measurements of electrostatic biopolymer adsorption onto chemically modified gold surfaces
    • Jordan CE, Corn RM. Surface plasmon resonance imaging measurements of electrostatic biopolymer adsorption onto chemically modified gold surfaces. Anal Chem. 69:1997;1449-1456.
    • (1997) Anal Chem , vol.69 , pp. 1449-1456
    • Jordan, C.E.1    Corn, R.M.2
  • 143
    • 0343058964 scopus 로고    scopus 로고
    • Viscoelastic properties of triacylglycerol interfaces covered by proteins
    • Benjamins J, Cagna A, Lucassen-Reynders EH. Viscoelastic properties of triacylglycerol interfaces covered by proteins. Colloid Surf A. 114:1996;245-254.
    • (1996) Colloid Surf a , vol.114 , pp. 245-254
    • Benjamins, J.1    Cagna, A.2    Lucassen-Reynders, E.H.3
  • 144
    • 0342502131 scopus 로고    scopus 로고
    • Adsorption of soluble proteins to dilating surfaces
    • Van Aken GA, Merks MTE. Adsorption of soluble proteins to dilating surfaces. Colloid Surf A. 114:1996;221-226.
    • (1996) Colloid Surf a , vol.114 , pp. 221-226
    • Van Aken, G.A.1    Merks, M.T.E.2
  • 145
    • 0030606339 scopus 로고    scopus 로고
    • Chemisorption of proteins and their thiol derivatives onto gold surfaces: Characterization based on electrochemical nonlinearity
    • Nakata S, Kido N, Hayashi M, Hara M, Sasabe H, Sugawara T, Matsuda T. Chemisorption of proteins and their thiol derivatives onto gold surfaces: characterization based on electrochemical nonlinearity. Biophys Chem. 62:1996;63-72.
    • (1996) Biophys Chem , vol.62 , pp. 63-72
    • Nakata, S.1    Kido, N.2    Hayashi, M.3    Hara, M.4    Sasabe, H.5    Sugawara, T.6    Matsuda, T.7
  • 146
    • 0030288097 scopus 로고    scopus 로고
    • The chronopotentiometric reduction of proteins adsorbed on mercury
    • Honeychurch MJ, Ridd MJ. The chronopotentiometric reduction of proteins adsorbed on mercury. J Electroanal Chem. 418:1996;185-194.
    • (1996) J Electroanal Chem , vol.418 , pp. 185-194
    • Honeychurch, M.J.1    Ridd, M.J.2
  • 147
    • 0011328355 scopus 로고    scopus 로고
    • When bivalent proteins might walk across cell surfaces
    • Vanden Broek W, Thompson NL. When bivalent proteins might walk across cell surfaces. J Phys Chem. 100:1996;11471-11479.
    • (1996) J Phys Chem , vol.100 , pp. 11471-11479
    • Vanden Broek, W.1    Thompson, N.L.2
  • 148
    • 0001098317 scopus 로고    scopus 로고
    • Lateral pressures in cell membranes: A mechanism for modulation of protein function
    • Membrane components may switch functions of proteins either by direct binding or, indirectly, through changes in properties of the bilayer. The latter mechanism is investigated by showing that minor changes in the transverse pressure profile within the bilayer may induce conformational transitions of embedded proteins.
    • Cantor RS. Lateral pressures in cell membranes: A mechanism for modulation of protein function. J Phys Chem B. 101:1997;1723-1725 Membrane components may switch functions of proteins either by direct binding or, indirectly, through changes in properties of the bilayer. The latter mechanism is investigated by showing that minor changes in the transverse pressure profile within the bilayer may induce conformational transitions of embedded proteins.
    • (1997) J Phys Chem B , vol.101 , pp. 1723-1725
    • Cantor, R.S.1
  • 149
    • 0001496226 scopus 로고    scopus 로고
    • A kinetic model of partially reversible protein absorption
    • Random sequential adsorption model for partially reversible binding of proteins. Adsorbed proteins are irreversibly bound only after going through a transition into a flat conformation. The model is capable of describing a number of common observations in protein adsorption, such as the adsorption kinetics and the irreversibly bound fraction of lysozome on silica
    • Van Tassel PR, Viot P, Tarjus G. A kinetic model of partially reversible protein absorption. J Chem Phys. 106:1997;761-770 Random sequential adsorption model for partially reversible binding of proteins. Adsorbed proteins are irreversibly bound only after going through a transition into a flat conformation. The model is capable of describing a number of common observations in protein adsorption, such as the adsorption kinetics and the irreversibly bound fraction of lysozome on silica.
    • (1997) J Chem Phys , vol.106 , pp. 761-770
    • Van Tassel, P.R.1    Viot, P.2    Tarjus, G.3
  • 152
    • 0029992051 scopus 로고    scopus 로고
    • Self-consistent-field modeling of adsorbed β-casein: Effects of pH and ionic strength on surface coverage and density profile
    • Self-consistent field modeling of a β-casein look-alike interacting with a solid wall. Treatment of the problem as the adsorption of a complex linear polyelectrolyte enables investigations of the influence of pH and ionic strength on the density profile.
    • Leermakers FAM, Atkinson PJ, Dickinson E, Home DS. Self-consistent-field modeling of adsorbed β-casein: Effects of pH and ionic strength on surface coverage and density profile. J Colloid Interface Sci. 178:1996;681-693 Self-consistent field modeling of a β-casein look-alike interacting with a solid wall. Treatment of the problem as the adsorption of a complex linear polyelectrolyte enables investigations of the influence of pH and ionic strength on the density profile.
    • (1996) J Colloid Interface Sci , vol.178 , pp. 681-693
    • Leermakers, F.A.M.1    Atkinson, P.J.2    Dickinson, E.3    Home, D.S.4
  • 153
    • 0030189525 scopus 로고    scopus 로고
    • Protein adsorption on lipid monolayers at their coexistence region
    • Describes the spatial distribution of proteins embedded into lipid surface monolayers in their phase coexistence regime from a mean-field free energy approach. Protein enrichment at the ordered/disordered lipid boundary line, a common experimental observation, is expected if the protein has no distinct preference for either lipid phase. A delocalization transition of the protein is predicted as the affinity of the protein to one of the phases is increased, for example, by variations of the temperature or protein concentration.
    • Netz RR, Andelman D, Orland H. Protein adsorption on lipid monolayers at their coexistence region. J Phys II. 6:1996;1023-1047 Describes the spatial distribution of proteins embedded into lipid surface monolayers in their phase coexistence regime from a mean-field free energy approach. Protein enrichment at the ordered/disordered lipid boundary line, a common experimental observation, is expected if the protein has no distinct preference for either lipid phase. A delocalization transition of the protein is predicted as the affinity of the protein to one of the phases is increased, for example, by variations of the temperature or protein concentration.
    • (1996) J Phys II , vol.6 , pp. 1023-1047
    • Netz, R.R.1    Andelman, D.2    Orland, H.3
  • 154
    • 0030915773 scopus 로고    scopus 로고
    • Significant role of electrostatic interactions for stabilization of protein assemblies
    • K. Nagayama, Ebashi G. Tokyo/Limerick: Japan Scientific Societies Press/Elsevier. (Series Editor): Advances in Biophysics
    • Takahashi T. Significant role of electrostatic interactions for stabilization of protein assemblies. Nagayama K, Ebashi G. Protein array: an alternate biomolecular system. 34:1997;41-54 Japan Scientific Societies Press/Elsevier, Tokyo/Limerick. (Series Editor): Advances in Biophysics.
    • (1997) Protein Array: An Alternate Biomolecular System , vol.34 , pp. 41-54
    • Takahashi, T.1
  • 155
    • 0002780411 scopus 로고    scopus 로고
    • CHASM (chain alignment on the surface of materials): An algorithm for predicting polymer and polypeptide conformations at interfaces
    • Reeves NJ, Evans JS. CHASM (chain alignment on the surface of materials): an algorithm for predicting polymer and polypeptide conformations at interfaces. J Phys Chem. 100:1996;17297-17304.
    • (1996) J Phys Chem , vol.100 , pp. 17297-17304
    • Reeves, N.J.1    Evans, J.S.2
  • 156
    • 0030582803 scopus 로고    scopus 로고
    • Origin of the anomalous diffusion observed by MD simulation at the protein-water interface
    • Bizzarri AR, Rocchi C, Cannistraro S. Origin of the anomalous diffusion observed by MD simulation at the protein-water interface. Chem Phys Lett. 263:1996;559-566.
    • (1996) Chem Phys Lett , vol.263 , pp. 559-566
    • Bizzarri, A.R.1    Rocchi, C.2    Cannistraro, S.3
  • 157
    • 33748587028 scopus 로고    scopus 로고
    • Antibiotic activity of valinomycin - molecular dynamics simulations involving the water/membrane interface
    • Detailed simulation of the cation shuttle, valinomycin, embedded in a hydrophobic/hydrophilic interface. Unbinding of potassium from the peptide has been observed in a rather short (100 psec) production run on ~19,000 atomic sites on a Cray T3D.
    • Forester TR, Smith W, Clarke JHR. Antibiotic activity of valinomycin - molecular dynamics simulations involving the water/membrane interface. J Chem Soc Faraday Trans. 93:1997;613-619 Detailed simulation of the cation shuttle, valinomycin, embedded in a hydrophobic/hydrophilic interface. Unbinding of potassium from the peptide has been observed in a rather short (100 psec) production run on ~19,000 atomic sites on a Cray T3D.
    • (1997) J Chem Soc Faraday Trans , vol.93 , pp. 613-619
    • Forester, T.R.1    Smith, W.2    Clarke, J.H.R.3
  • 158
    • 0001707522 scopus 로고    scopus 로고
    • Electrochemical patterning of self-assembled monolayers onto microscopic arrays of gold electrodes fabricated by laser ablation
    • Tender LM, Worley RL, Fan H-Y, Lopez GP. Electrochemical patterning of self-assembled monolayers onto microscopic arrays of gold electrodes fabricated by laser ablation. Langmuir. 12:1996;5515-5518.
    • (1996) Langmuir , vol.12 , pp. 5515-5518
    • Tender, L.M.1    Worley, R.L.2    Fan H-Y3    Lopez, G.P.4
  • 159
    • 0000344267 scopus 로고    scopus 로고
    • Modified DNA immobilized on bioreactive self-assembled monolayer on gold for dynamic force microscopy imaging in aqueous buffer solution
    • Hegner M, Dreier M, Wagner P, Semenza G, Güntherodt HJ. Modified DNA immobilized on bioreactive self-assembled monolayer on gold for dynamic force microscopy imaging in aqueous buffer solution. J Vac Sci Technol B. 14:1996;1418-1421.
    • (1996) J Vac Sci Technol B , vol.14 , pp. 1418-1421
    • Hegner, M.1    Dreier, M.2    Wagner, P.3    Semenza, G.4    Güntherodt, H.J.5


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