메뉴 건너뛰기




Volumn 61, Issue 2, 2005, Pages 385-397

Structure and stability of a model three-helix-bundle protein on tailored surfaces

Author keywords

Density of states; Expanded ensemble; G model; Mechanical stretching; Monte Carlo simulation

Indexed keywords

BACTERIAL PROTEIN; PROTEIN A;

EID: 26444593315     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20581     Document Type: Article
Times cited : (33)

References (67)
  • 1
    • 1342302795 scopus 로고    scopus 로고
    • The interaction of proteins with solid surfaces
    • Gray JJ. The interaction of proteins with solid surfaces. Curr Opin Struct Biol 2004;14:110-115.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 110-115
    • Gray, J.J.1
  • 3
    • 0006224786 scopus 로고
    • Films of protein in bilogical processes
    • Rothen A. Films of protein in bilogical processes. Adv Protein Chem 1947;3:123-137.
    • (1947) Adv Protein Chem , vol.3 , pp. 123-137
    • Rothen, A.1
  • 4
    • 0001475945 scopus 로고
    • Physicochemical and biological aspects of proteins at interfaces
    • Chessman DF, Davies JT. Physicochemical and biological aspects of proteins at interfaces. Adv Protein Chem 1954;9:439-501.
    • (1954) Adv Protein Chem , vol.9 , pp. 439-501
    • Chessman, D.F.1    Davies, J.T.2
  • 5
    • 0035060814 scopus 로고    scopus 로고
    • On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon
    • Nakanishi Z, Sakiyama T, Imamura K. On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon. J Biosci Bioeng 2001;91:233-244.
    • (2001) J Biosci Bioeng , vol.91 , pp. 233-244
    • Nakanishi, Z.1    Sakiyama, T.2    Imamura, K.3
  • 6
    • 0002091980 scopus 로고
    • Structural changes of T4 lysozyme upon adsoprtion to silica nanoparticles measured by circular dichroism
    • Billsten P, Wahlgren M, Arnebrant T, McGuire J, Elwing H. Structural changes of T4 lysozyme upon adsoprtion to silica nanoparticles measured by circular dichroism. J Colloid Interface Sci 1995;175:77-32.
    • (1995) J Colloid Interface Sci , vol.175 , pp. 77-132
    • Billsten, P.1    Wahlgren, M.2    Arnebrant, T.3    McGuire, J.4    Elwing, H.5
  • 7
    • 0035862841 scopus 로고    scopus 로고
    • Effect of temperature on the conformation of lyzozyme adsorbed to silica particles
    • Czeslik C, Winter R. Effect of temperature on the conformation of lyzozyme adsorbed to silica particles. Phys Chem Chem Phys 2001;3:235-239.
    • (2001) Phys Chem Chem Phys , vol.3 , pp. 235-239
    • Czeslik, C.1    Winter, R.2
  • 9
    • 0028274435 scopus 로고
    • Cysteine-specific surface tethering of genetically engineered cytochromes for fabrication of metalloprotein nanostructures
    • Hong H-G, Jiang M, Sligar SG, Bohn PW. Cysteine-specific surface tethering of genetically engineered cytochromes for fabrication of metalloprotein nanostructures. Langmuir 1994;10:153-158.
    • (1994) Langmuir , vol.10 , pp. 153-158
    • Hong, H.-G.1    Jiang, M.2    Sligar, S.G.3    Bohn, P.W.4
  • 10
    • 0030948781 scopus 로고    scopus 로고
    • Patterned delivery of immunoglobulins to surfaces using microfluidic networks
    • Delamarche E, Bernard A, Schmid H, Michel B, Biebuyck H. Patterned delivery of immunoglobulins to surfaces using microfluidic networks. Science 1997;276:779-781.
    • (1997) Science , vol.276 , pp. 779-781
    • Delamarche, E.1    Bernard, A.2    Schmid, H.3    Michel, B.4    Biebuyck, H.5
  • 11
    • 0032573880 scopus 로고    scopus 로고
    • Microfluidic networks for chemical patterning of substrates: Design and application to bioassays
    • Delamarche E, Bernard A, Schmid H, Bietsch A, Michel B, Biebuyck H. Microfluidic networks for chemical patterning of substrates: Design and application to bioassays. J Am Chem Soc 1998;120:500-508.
    • (1998) J Am Chem Soc , vol.120 , pp. 500-508
    • Delamarche, E.1    Bernard, A.2    Schmid, H.3    Bietsch, A.4    Michel, B.5    Biebuyck, H.6
  • 12
    • 0026351910 scopus 로고
    • Self-assembled organic monolayers: Model systems for studying adsorption of proteins at surfaces
    • Prime KL, Whitesides GM. Self-assembled organic monolayers: model systems for studying adsorption of proteins at surfaces. Science 1991;252:1164-1167.
    • (1991) Science , vol.252 , pp. 1164-1167
    • Prime, K.L.1    Whitesides, G.M.2
  • 13
    • 12044254336 scopus 로고
    • Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide): A model system using self-assembled monolayers
    • Prime KL, Whitesides GM. Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide): a model system using self-assembled monolayers. J Am Chem Soc 1993;115:10714-10721.
    • (1993) J Am Chem Soc , vol.115 , pp. 10714-10721
    • Prime, K.L.1    Whitesides, G.M.2
  • 14
    • 0029185755 scopus 로고
    • Biospecific adsorption of carbonic anhydrase to self-assembled monlayers of alkanethiolates that present benzenesulfonamide groups on gold
    • Mrksich M, Grunwell JR, Whitesides GM. Biospecific adsorption of carbonic anhydrase to self-assembled monlayers of alkanethiolates that present benzenesulfonamide groups on gold. J Am Chem Soc 1995;117:12009-12010.
    • (1995) J Am Chem Soc , vol.117 , pp. 12009-12010
    • Mrksich, M.1    Grunwell, J.R.2    Whitesides, G.M.3
  • 15
    • 0032799596 scopus 로고    scopus 로고
    • The interactions of proteins and cells with self-assembled monolayers of alkanethiolates on gold and silver
    • Ostuni E, Yan L, Whitesides GM. The interactions of proteins and cells with self-assembled monolayers of alkanethiolates on gold and silver. Coll Surf B 1999;15:3-30.
    • (1999) Coll Surf B , vol.15 , pp. 3-30
    • Ostuni, E.1    Yan, L.2    Whitesides, G.M.3
  • 16
    • 0037418426 scopus 로고    scopus 로고
    • Adsorption of proteins to hydrophobic sites on mixed self-assembled monolayers
    • Ostuni E, Grzybowski BA, Mrksich M, Roberts CS, Whitesides GM. Adsorption of proteins to hydrophobic sites on mixed self-assembled monolayers. Langumir 2003;19:1861-1872.
    • (2003) Langumir , vol.19 , pp. 1861-1872
    • Ostuni, E.1    Grzybowski, B.A.2    Mrksich, M.3    Roberts, C.S.4    Whitesides, G.M.5
  • 18
  • 19
    • 0030026989 scopus 로고    scopus 로고
    • Protein adsoprtion on solid surfaces
    • Hlady V, Buijs J. Protein adsoprtion on solid surfaces. Curr Opin Biotech 1996;7:72-77.
    • (1996) Curr Opin Biotech , vol.7 , pp. 72-77
    • Hlady, V.1    Buijs, J.2
  • 20
    • 0037013360 scopus 로고    scopus 로고
    • A brownian dynamics study of the initial stages of hen egg-white lysozyme adsorption at a solid interface
    • Ravichandran S, Madura JD, Talbot J. A brownian dynamics study of the initial stages of hen egg-white lysozyme adsorption at a solid interface. J Phys Chem B 2001;105:3610-3613.
    • (2001) J Phys Chem B , vol.105 , pp. 3610-3613
    • Ravichandran, S.1    Madura, J.D.2    Talbot, J.3
  • 21
    • 0037047209 scopus 로고    scopus 로고
    • Effect of molecular structure on the adsorption of protein on surfaces with grafted polymers
    • Fang F, Szleifer I. Effect of molecular structure on the adsorption of protein on surfaces with grafted polymers. Langmuir 2002;18: 5497-5510.
    • (2002) Langmuir , vol.18 , pp. 5497-5510
    • Fang, F.1    Szleifer, I.2
  • 22
    • 0000964469 scopus 로고
    • Modeling of protein adsorption on polymer surfaces. Computation of adsorption potential
    • Noinville V, Vidal-Madjar C, Sébille, B. Modeling of protein adsorption on polymer surfaces. Computation of adsorption potential. J Phys Chem 1995;99:1516-1522.
    • (1995) J Phys Chem , vol.99 , pp. 1516-1522
    • Noinville, V.1    Vidal-Madjar, C.2    Sébille, B.3
  • 23
    • 0037447025 scopus 로고    scopus 로고
    • Simulation study of the interaction of some albumin subdomains with a flat graphite surface
    • Raffaini G, Ganazzoli F. Simulation study of the interaction of some albumin subdomains with a flat graphite surface. Langmuir 2003;19:3403-3412.
    • (2003) Langmuir , vol.19 , pp. 3403-3412
    • Raffaini, G.1    Ganazzoli, F.2
  • 24
    • 5444268689 scopus 로고    scopus 로고
    • Molecular simulation study of water interactions with oligo (ethylene glycol)-terminated alkanethiol self-assembled monolayers
    • Zheng J, Li L, Chen S, Jiang S. Molecular simulation study of water interactions with oligo (ethylene glycol)-terminated alkanethiol self-assembled monolayers. Langmuir 2004;20:8931-8938.
    • (2004) Langmuir , vol.20 , pp. 8931-8938
    • Zheng, J.1    Li, L.2    Chen, S.3    Jiang, S.4
  • 25
    • 0029151245 scopus 로고
    • First-principles calculation of the folding free energy of a three-helix bundle protein
    • Boczko EM, Brooks III CL. First-principles calculation of the folding free energy of a three-helix bundle protein. Science 1995; 269:393-396.
    • (1995) Science , vol.269 , pp. 393-396
    • Boczko, E.M.1    Brooks III, C.L.2
  • 26
    • 0030967896 scopus 로고    scopus 로고
    • Exploring the folding free energy surface of a three-helix bundle protein
    • Guo Z, Brooks III CL, Boczko EM. Exploring the folding free energy surface of a three-helix bundle protein. PNAS 1997;94: 10161-10166.
    • (1997) PNAS , vol.94 , pp. 10161-10166
    • Guo, Z.1    Brooks III, C.L.2    Boczko, E.M.3
  • 27
    • 0031475159 scopus 로고    scopus 로고
    • Folding thermodynamics of a model three-helix-bundle protein
    • Zhou Y, Karplus M. Folding thermodynamics of a model three-helix-bundle protein. PNAS 1997;94:14429-14432.
    • (1997) PNAS , vol.94 , pp. 14429-14432
    • Zhou, Y.1    Karplus, M.2
  • 28
    • 0033607208 scopus 로고    scopus 로고
    • Exploring the origins of topological frustration: Design of a minimally frustrated model of fragment B of protein A
    • Shea J, Onuchic JN, Brooks III CL. Exploring the origins of topological frustration: design of a minimally frustrated model of fragment B of protein A. PNAS 1999;96:12512-12517.
    • (1999) PNAS , vol.96 , pp. 12512-12517
    • Shea, J.1    Onuchic, J.N.2    Brooks III, C.L.3
  • 29
    • 0034602807 scopus 로고    scopus 로고
    • Staphylococcal protein A: Unfolding pathways, unfolded states, and differences between the B and E domains
    • Alonso DOV, Daggett V. Staphylococcal protein A: unfolding pathways, unfolded states, and differences between the B and E domains. PNAS 2000;97:133-138.
    • (2000) PNAS , vol.97 , pp. 133-138
    • Alonso, D.O.V.1    Daggett, V.2
  • 30
    • 0345133287 scopus 로고    scopus 로고
    • Folding a protein in a computer: An atomic description of the folding/unfolding of protein A
    • García AE, Onuchic JN. Folding a protein in a computer: an atomic description of the folding/unfolding of protein A. PNAS 2003;100:13898-13903.
    • (2003) PNAS , vol.100 , pp. 13898-13903
    • García, A.E.1    Onuchic, J.N.2
  • 31
    • 0026801084 scopus 로고
    • Three-dimensional solution structure of the B domain of Staphylococcal protein A: Comparisons of the solution and crystal structures
    • Gouda H, Torigoe H, Saito A, Sato M, Arata Y, Shimada I. Three-dimensional solution structure of the B domain of Staphylococcal protein A: comparisons of the solution and crystal structures. Biochemistry 1992;31:9665-9672.
    • (1992) Biochemistry , vol.31 , pp. 9665-9672
    • Gouda, H.1    Torigoe, H.2    Saito, A.3    Sato, M.4    Arata, Y.5    Shimada, I.6
  • 32
    • 0037062480 scopus 로고    scopus 로고
    • Simulations of β-hairpin folding confined to spherical pores using distributed computing
    • Klimov DK, Newfield D, Thirumalai D. Simulations of β-hairpin folding confined to spherical pores using distributed computing. PNAS 2002;99:8019-8024.
    • (2002) PNAS , vol.99 , pp. 8019-8024
    • Klimov, D.K.1    Newfield, D.2    Thirumalai, D.3
  • 33
    • 0141482088 scopus 로고    scopus 로고
    • How protein thermodynamics and folding mechanisms are altered by the caperonin cage: Molecular simulations
    • Takagi F, Koga N, Takada S. How protein thermodynamics and folding mechanisms are altered by the caperonin cage: molecular simulations. PNAS 2003;100:11367-11372.
    • (2003) PNAS , vol.100 , pp. 11367-11372
    • Takagi, F.1    Koga, N.2    Takada, S.3
  • 34
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Gō N. Theoretical studies of protein folding. Annu Rev Biophys Bioeng 1983;12:183-210.
    • (1983) Annu Rev Biophys Bioeng , vol.12 , pp. 183-210
    • Go, N.1
  • 35
    • 0032443390 scopus 로고    scopus 로고
    • Discrete molecular dynamics studies of the folding of a protein-like model
    • Dokholyan NV, Buldyrev SV, Stanley HE, Shakhnovick EI. Discrete molecular dynamics studies of the folding of a protein-like model. Fold Des 1998;3:377-387.
    • (1998) Fold Des , vol.3 , pp. 377-387
    • Dokholyan, N.V.1    Buldyrev, S.V.2    Stanley, H.E.3    Shakhnovick, E.I.4
  • 36
    • 0001720011 scopus 로고    scopus 로고
    • Molecular dynamics of folding of secondary structures in Gō-type models of proteins
    • Hoang TX, Cieplak M. Molecular dynamics of folding of secondary structures in Gō-type models of proteins. J Chem Phys 2000;112: 6851-6862.
    • (2000) J Chem Phys , vol.112 , pp. 6851-6862
    • Hoang, T.X.1    Cieplak, M.2
  • 37
    • 0034319711 scopus 로고    scopus 로고
    • Sequencing of folding events in Gō-type proteins
    • Hoang TX, Cieplak M. Sequencing of folding events in Gō-type proteins. J Chem Phys 2000;113:8319-8328.
    • (2000) J Chem Phys , vol.113 , pp. 8319-8328
    • Hoang, T.X.1    Cieplak, M.2
  • 38
    • 0035850732 scopus 로고    scopus 로고
    • Roles of native topology and chain-length scaling in protein folding: A simulation study with a Gō-like model
    • Koga N, Takada S. Roles of native topology and chain-length scaling in protein folding: a simulation study with a Gō-like model. J Mol Biol 2001;313:171-180.
    • (2001) J Mol Biol , vol.313 , pp. 171-180
    • Koga, N.1    Takada, S.2
  • 39
  • 40
    • 0037216990 scopus 로고    scopus 로고
    • Universality classes in folding times of proteins
    • Cieplak M, Hoang TX. Universality classes in folding times of proteins. Biophys J 2003;84:475-488.
    • (2003) Biophys J , vol.84 , pp. 475-488
    • Cieplak, M.1    Hoang, T.X.2
  • 41
    • 0242383943 scopus 로고    scopus 로고
    • Improved Gō-like models demonstrate the robustness of protein folding mechanisms towards non-native interactions
    • Karanicolas J, Brooks III CL. Improved Gō-like models demonstrate the robustness of protein folding mechanisms towards non-native interactions. J Mol Biol 2003;334:309-325.
    • (2003) J Mol Biol , vol.334 , pp. 309-325
    • Karanicolas, J.1    Brooks III, C.L.2
  • 43
    • 0036783398 scopus 로고    scopus 로고
    • Folding and stretching in a Gō-like model of titin
    • Cieplak M, Hoang TX, Robbins MO. Folding and stretching in a Gō-like model of titin. Proteins 2002;49:114-124.
    • (2002) Proteins , vol.49 , pp. 114-124
    • Cieplak, M.1    Hoang, T.X.2    Robbins, M.O.3
  • 44
    • 0032742688 scopus 로고    scopus 로고
    • Gō-ing for the prediction of protein folding mechanisms
    • Takada S. Gō-ing for the prediction of protein folding mechanisms. PNAS 1999;96:11698-11700.
    • (1999) PNAS , vol.96 , pp. 11698-11700
    • Takada, S.1
  • 45
    • 0035400210 scopus 로고    scopus 로고
    • Kinetic nonoptimality and vibrational stability of proteins
    • Cieplak M, Hoang TX. Kinetic nonoptimality and vibrational stability of proteins. Proteins 2001;44:22-25.
    • (2001) Proteins , vol.44 , pp. 22-25
    • Cieplak, M.1    Hoang, T.X.2
  • 46
    • 0037459035 scopus 로고    scopus 로고
    • Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: How adequate is native-centric topological modeling
    • Kaya H, Chan HS. Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: how adequate is native-centric topological modeling. J Mol Biol 2003;326:911-931.
    • (2003) J Mol Biol , vol.326 , pp. 911-931
    • Kaya, H.1    Chan, H.S.2
  • 47
    • 1542319916 scopus 로고    scopus 로고
    • Cooperativity principles in protein folding
    • Chan HS, Shimizu S, Kaya H. Cooperativity principles in protein folding. Methods Enzymol 2004;380:350-379.
    • (2004) Methods Enzymol , vol.380 , pp. 350-379
    • Chan, H.S.1    Shimizu, S.2    Kaya, H.3
  • 48
    • 22944453404 scopus 로고    scopus 로고
    • Optimal allocation of replicas in parallel temperating simulations
    • Rathore N, Chopra M, de Pablo JJ. Optimal allocation of replicas in parallel temperating simulations. J Chem Phys 2005;122: 024111.
    • (2005) J Chem Phys , vol.122 , pp. 024111
    • Rathore, N.1    Chopra, M.2    De Pablo, J.J.3
  • 49
    • 36449000062 scopus 로고
    • Nose-Hoover chains: The canonical ensemble via continuous dynamics
    • Martyna GJ, Klein ML, Tuckerman M. Nose-Hoover chains: the canonical ensemble via continuous dynamics. J Chem Phys 1992; 97:2635-2643.
    • (1992) J Chem Phys , vol.97 , pp. 2635-2643
    • Martyna, G.J.1    Klein, M.L.2    Tuckerman, M.3
  • 50
    • 6644221271 scopus 로고    scopus 로고
    • Efficient, multiple-range random walk algorithm to calculate the density of states
    • Wang F, Landau DP. Efficient, multiple-range random walk algorithm to calculate the density of states. Phys Rev Lett 2001;86:2050-2053.
    • (2001) Phys Rev Lett , vol.86 , pp. 2050-2053
    • Wang, F.1    Landau, D.P.2
  • 51
    • 39749147672 scopus 로고    scopus 로고
    • Determining the density of states for classical statistical models: A random walk algorithm to produce a flat histogram
    • Wang F, Landau DP. Determining the density of states for classical statistical models: a random walk algorithm to produce a flat histogram. Phys Rev E 2001;64:056101-056116.
    • (2001) Phys Rev E , vol.64 , pp. 56101-56116
    • Wang, F.1    Landau, D.P.2
  • 52
    • 0037156112 scopus 로고    scopus 로고
    • Monte Carlo simulation of proteins through a random walk in energy space
    • Rathore N, de Pablo JJ. Monte Carlo simulation of proteins through a random walk in energy space. J Chem Phys 2002;116: 7225-7230.
    • (2002) J Chem Phys , vol.116 , pp. 7225-7230
    • Rathore, N.1    De Pablo, J.J.2
  • 54
    • 0344118922 scopus 로고    scopus 로고
    • Configurational temperature density of states simulations of proteins
    • Rathore N, Knotts IV TA, de Pablo JJ. Configurational temperature density of states simulations of proteins. Biophys J 2003;85: 3963-3968.
    • (2003) Biophys J , vol.85 , pp. 3963-3968
    • Rathore, N.1    Knotts IV, T.A.2    De Pablo, J.J.3
  • 55
    • 0037159430 scopus 로고    scopus 로고
    • Potential of mean force between a spherical particle suspended in a nematic liquid crystal and a substrate
    • Kim EB, Faller R, Yan Q, Abbott NL, de Pablo JJ. Potential of mean force between a spherical particle suspended in a nematic liquid crystal and a substrate. J Chem Phys 2002;117:7781-7787.
    • (2002) J Chem Phys , vol.117 , pp. 7781-7787
    • Kim, E.B.1    Faller, R.2    Yan, Q.3    Abbott, N.L.4    De Pablo, J.J.5
  • 56
    • 1942535023 scopus 로고    scopus 로고
    • Molecular simulation of the reversible mechanical unfolding of proteins
    • Rathore N, Yan Q, de Pablo JJ. Molecular simulation of the reversible mechanical unfolding of proteins. J Chem Phys 2004;120: 5781-5788.
    • (2004) J Chem Phys , vol.120 , pp. 5781-5788
    • Rathore, N.1    Yan, Q.2    De Pablo, J.J.3
  • 58
    • 0034284366 scopus 로고    scopus 로고
    • Modeling protein density of states: Additive hydrophobic effects are insufficient for calorimetric two-state cooperativity
    • Chan HS. Modeling protein density of states: additive hydrophobic effects are insufficient for calorimetric two-state cooperativity. Proteins 2000;40:543-571.
    • (2000) Proteins , vol.40 , pp. 543-571
    • Chan, H.S.1
  • 59
    • 0031214657 scopus 로고    scopus 로고
    • Competing interactions and levels of ordering in self-organizing polymeric materials
    • Muthukumar M, Ober CK, Thomas EL. Competing interactions and levels of ordering in self-organizing polymeric materials. Science 1997;277:1225-1232.
    • (1997) Science , vol.277 , pp. 1225-1232
    • Muthukumar, M.1    Ober, C.K.2    Thomas, E.L.3
  • 60
    • 0027318781 scopus 로고
    • Kinetics and thermodynamics of folding in model proteins
    • Camacho CJ, Thirumalai D. Kinetics and thermodynamics of folding in model proteins. PNAS 1993;90:6369-6372.
    • (1993) PNAS , vol.90 , pp. 6369-6372
    • Camacho, C.J.1    Thirumalai, D.2
  • 61
    • 0001669870 scopus 로고
    • Kinetic and thermodynamic analysis of proteinlike heteropolymers: Monte Carlo histogram technique
    • Socci ND, Onuchic JN. Kinetic and thermodynamic analysis of proteinlike heteropolymers: Monte Carlo histogram technique. J Chem Phys 1995;103:4732-4744.
    • (1995) J Chem Phys , vol.103 , pp. 4732-4744
    • Socci, N.D.1    Onuchic, J.N.2
  • 62
    • 4243572706 scopus 로고    scopus 로고
    • Criterion that determines the foldability of proteins
    • Klimov DK, Thirumalai D. Criterion that determines the foldability of proteins. Phys Rev Lett 1996;76:4070-4073.
    • (1996) Phys Rev Lett , vol.76 , pp. 4070-4073
    • Klimov, D.K.1    Thirumalai, D.2
  • 63
    • 0034284060 scopus 로고    scopus 로고
    • Polymer principles of protein calorimetric two-state cooperativity
    • Kaya H, Chan HS. Polymer principles of protein calorimetric two-state cooperativity. Proteins 2000;40:637-661.
    • (2000) Proteins , vol.40 , pp. 637-661
    • Kaya, H.1    Chan, H.S.2
  • 64
    • 0028608099 scopus 로고
    • The stability and unfolding of an IgG binding protein based upon the B domain of protein A from Staphylococcus aureus probed by tryptophan substitution and fluorescence spectroscopy
    • Bottomley SP, Popplewell AG, Scawen M, Wan T, Sutton BJ, Gore MG. The stability and unfolding of an IgG binding protein based upon the B domain of protein A from Staphylococcus aureus probed by tryptophan substitution and fluorescence spectroscopy. Protein Eng 1994;7:1463-1470.
    • (1994) Protein Eng , vol.7 , pp. 1463-1470
    • Bottomley, S.P.1    Popplewell, A.G.2    Scawen, M.3    Wan, T.4    Sutton, B.J.5    Gore, M.G.6
  • 65
    • 0029904435 scopus 로고    scopus 로고
    • Minimizing a binding domain from protein A
    • Braisted AC, Wells JA. Minimizing a binding domain from protein A. PNAS 1996;93:5688-5692.
    • (1996) PNAS , vol.93 , pp. 5688-5692
    • Braisted, A.C.1    Wells, J.A.2
  • 67
    • 0030755502 scopus 로고    scopus 로고
    • Absence of a stable intermediate on the folding pathway of protein A
    • Bai Y, Karimi A, Dyson HJ, Wright PE. Absence of a stable intermediate on the folding pathway of protein A. Protein Sci 1997;6:1449-1457.
    • (1997) Protein Sci , vol.6 , pp. 1449-1457
    • Bai, Y.1    Karimi, A.2    Dyson, H.J.3    Wright, P.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.