메뉴 건너뛰기




Volumn 24, Issue 3, 2011, Pages 490-502

Single and multiple bonds in (strept)avidin-biotin interactions

Author keywords

atomic force microscopy (AFM); avidin; biotin; interaction; lifetime; multiple bond; single bond; streptavidin

Indexed keywords

AVIDIN; BIOTIN; STREPTAVIDIN;

EID: 79955093445     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.1109     Document Type: Article
Times cited : (72)

References (78)
  • 1
    • 0026829635 scopus 로고
    • Operational aspects of antibody affinity constants measured by liquid-phase and solid-phase assays
    • Azimzadeh A, Pellequer JL, Van Regenmortel MHV., 1992. Operational aspects of antibody affinity constants measured by liquid-phase and solid-phase assays. J. Mol. Recognit. 5: 9-18.
    • (1992) J. Mol. Recognit. , vol.5 , pp. 9-18
    • Azimzadeh, A.1    Pellequer, J.L.2    Van Regenmortel, M.H.V.3
  • 2
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell GI., 1978. Models for the specific adhesion of cells to cells. Science 200: 618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 4
    • 69049092626 scopus 로고    scopus 로고
    • Methods and estimations of uncertainties in single-molecule dynamic force spectroscopy
    • Björnham O, Schedin S., 2009. Methods and estimations of uncertainties in single-molecule dynamic force spectroscopy. Eur. Biophys. J. 38: 911-922.
    • (2009) Eur. Biophys. J. , vol.38 , pp. 911-922
    • Björnham, O.1    Schedin, S.2
  • 5
    • 33750604650 scopus 로고    scopus 로고
    • Antibodies with infinite affinity: Origins and applications
    • Butlin NG, Meares CF., 2006. Antibodies with infinite affinity: origins and applications. Acc. Chem. Res. 39: 780-787.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 780-787
    • Butlin, N.G.1    Meares, C.F.2
  • 6
    • 0028853559 scopus 로고
    • The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy
    • Chilkoti A, Boland T, Ratner BD, Stayton PS., 1995. The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy. Biophys. J. 69: 2125-2130.
    • (1995) Biophys. J. , vol.69 , pp. 2125-2130
    • Chilkoti, A.1    Boland, T.2    Ratner, B.D.3    Stayton, P.S.4
  • 9
    • 0000354225 scopus 로고    scopus 로고
    • Force spectroscopy and dynamics of the biotin-avidin bond studied by scanning force microscopy
    • DeParis R, Strunz T, Oroszlan K, Güntherodt H-J, Hegner M., 2000. Force spectroscopy and dynamics of the biotin-avidin bond studied by scanning force microscopy. Single Mol. 1: 285-290.
    • (2000) Single Mol. , vol.1 , pp. 285-290
    • Deparis, R.1    Strunz, T.2    Oroszlan, K.3    Güntherodt, H.-J.4    Hegner, M.5
  • 10
    • 1542375742 scopus 로고    scopus 로고
    • Effects of Intermediate Bound States in Dynamic Force Spectroscopy
    • Derenyi I, Bartolo D, Ajdari A., 2004. Effects of intermediate bound states in dynamic force spectroscopy. Biophys. J. 86: 1263-1269. (Pubitemid 38295568)
    • (2004) Biophysical Journal , vol.86 , Issue.3 , pp. 1263-1269
    • Derenyi, I.1    Bartolo, D.2    Ajdari, A.3
  • 11
    • 0009934025 scopus 로고
    • The structure of biotin
    • du Vigneaud V., 1942. The structure of biotin. Science 96: 455-461.
    • (1942) Science , vol.96 , pp. 455-461
    • Du Vigneaud, V.1
  • 13
    • 77950613901 scopus 로고
    • A constituent of raw egg white capable of inactivating biotin in vitro
    • Eakin RE, Snell EE, Williams RJ., 1940. A constituent of raw egg white capable of inactivating biotin in vitro. J. Biol. Chem. 136: 801-802.
    • (1940) J. Biol. Chem. , vol.136 , pp. 801-802
    • Eakin, R.E.1    Snell, E.E.2    Williams, R.J.3
  • 15
    • 79051470983 scopus 로고    scopus 로고
    • Dynamic force spectroscopy on multiple bonds: Experiments and model
    • Erdmann T, Pierrat S, Nassoy P, Schwarz US., 2008. Dynamic force spectroscopy on multiple bonds: experiments and model Europhys. Lett. 81: 48001.
    • (2008) Europhys. Lett. , vol.81 , pp. 48001
    • Erdmann, T.1    Pierrat, S.2    Nassoy, P.3    Schwarz, U.S.4
  • 16
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans E, Ritchie K., 1997. Dynamic strength of molecular adhesion bonds. Biophys. J. 72: 1541-1555. (Pubitemid 27133095)
    • (1997) Biophysical Journal , vol.72 , Issue.4 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 17
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin EL, Moy VT, Gaub HE., 1994. Adhesion forces between individual ligand-receptor pairs. Science 264: 415-417. (Pubitemid 24179839)
    • (1994) Science , vol.264 , Issue.5157 , pp. 415-417
    • Florin, E.-L.1    Moy, V.T.2    Gaub, H.E.3
  • 18
    • 0032577315 scopus 로고    scopus 로고
    • Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex
    • DOI 10.1006/jmbi.1998.1735
    • Freitag S, Le Trong I, Chilkoti A, Klumb LA, Stayton PS, Stenkamp RE., 1998. Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex. J. Mol. Biol. 279: 211-221. (Pubitemid 28252140)
    • (1998) Journal of Molecular Biology , vol.279 , Issue.1 , pp. 211-221
    • Freitag, S.1    Le Trong, I.2    Chilkoti, A.3    Klumb, L.A.4    Stayton, P.S.5    Stenkamp, R.E.6
  • 19
    • 0037621477 scopus 로고    scopus 로고
    • Dynamic single-molecule force spectroscopy: Bond rupture analysis with variable spacer length
    • Friedsam C, Wehle AK, Kühner F, Gaub H., 2003. Dynamic single-molecule force spectroscopy: bond rupture analysis with variable spacer length. J. Phys. Condens. Matter 15: 1709-1723.
    • (2003) J. Phys. Condens. Matter , vol.15 , pp. 1709-1723
    • Friedsam, C.1    Wehle, A.K.2    Kühner, F.3    Gaub, H.4
  • 21
    • 78349292832 scopus 로고
    • Avidin. 1. the use of (14-C)biotin for kinetic studies and for assay
    • Green NM., 1963a. Avidin. 1. The use of (14-C)biotin for kinetic studies and for assay. Biochem. J. 89: 585-591.
    • (1963) Biochem. J. , vol.89 , pp. 585-591
    • Green, N.M.1
  • 22
    • 0000225469 scopus 로고
    • Avidin. 3. the nature of the biotin-binding site
    • Green NM., 1963b. Avidin. 3. The nature of the biotin-binding site. Biochem. J. 89: 599-609.
    • (1963) Biochem. J. , vol.89 , pp. 599-609
    • Green, N.M.1
  • 23
    • 0001071988 scopus 로고
    • Avidin. 4. Stability at extremes of pH and dissociation into sub-units by guanidine hydrochloride
    • Green NM., 1963c. Avidin. 4. Stability at extremes of pH and dissociation into sub-units by guanidine hydrochloride. Biochem. J. 89: 609-620.
    • (1963) Biochem. J. , vol.89 , pp. 609-620
    • Green, N.M.1
  • 25
    • 77952373558 scopus 로고    scopus 로고
    • Distributions of parameters and features of multiple bond ruptures in force spectroscopy by atomic force microscopy
    • Guo S., 2010. Distributions of parameters and features of multiple bond ruptures in force spectroscopy by atomic force microscopy. J. Phys. Chem. C 114: 8755-8765.
    • (2010) J. Phys. Chem. C , vol.114 , pp. 8755-8765
    • Guo, S.1
  • 26
    • 56049083274 scopus 로고    scopus 로고
    • Effects of multiple-bond ruptures on kinetic parameters extracted from force spectroscopy measurements: Revisiting biotin-streptavidin interactions
    • Guo S, Ray C, Kirkpatrick A, Lad N, Akhremitchev B., 2008. Effects of multiple-bond ruptures on kinetic parameters extracted from force spectroscopy measurements: revisiting biotin-streptavidin interactions. Biophys. J. 95: 3964-3976.
    • (2008) Biophys. J. , vol.95 , pp. 3964-3976
    • Guo, S.1    Ray, C.2    Kirkpatrick, A.3    Lad, N.4    Akhremitchev, B.5
  • 27
    • 0034948356 scopus 로고    scopus 로고
    • The rules are changing: Force measurements on single molecules and how they relate to bulk reaction kinetics and energies
    • DOI 10.1023/A:1011408900407
    • Guthold M, Superfine R, Taylor RM., 2001. The rules are changing: force measurements on single molecule and how they relate to bulk reaction kinetics and energies. Biomed. Microdevices 3: 9-18. (Pubitemid 32655105)
    • (2001) Biomedical Microdevices , vol.3 , Issue.1 , pp. 9-18
    • Guthold, M.1    Superfine, R.2    Taylor II, R.M.3
  • 29
    • 14944364973 scopus 로고    scopus 로고
    • The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures
    • DOI 10.1002/elps.200410070
    • Holmberg A, Blomstergren A, Nord O, Lukacs M, Lundeberg J, Uhlen M., 2005. The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures. Electrophoresis 26: 501-510. (Pubitemid 40372776)
    • (2005) Electrophoresis , vol.26 , Issue.3 , pp. 501-510
    • Holmberg, A.1    Blomstergren, A.2    Nord, O.3    Lukacs, M.4    Lundeberg, J.5    Uhlen, M.6
  • 31
    • 27744586032 scopus 로고    scopus 로고
    • Multiple-bond kinetics from single-molecule pulling experiments: Evidence for multiple NCAM bonds
    • DOI 10.1529/biophysj.105.061606
    • Hukkanen EJ, Wieland JA, Gewirth A, Leckband DE, Braatz RD., 2005. Multiple-bond kinetics from single-molecule pulling experiments: evidence for multiple NCAM bonds. Biophys. J. 89: 3434-3445. (Pubitemid 41636098)
    • (2005) Biophysical Journal , vol.89 , Issue.5 , pp. 3434-3445
    • Hukkanen, E.J.1    Wieland, J.A.2    Gewirth, A.3    Leckband, D.E.4    Braatz, R.D.5
  • 35
    • 5644291496 scopus 로고
    • Uber das bios-problem: Darstellung von krystallisiertem Biotin aus eigelb
    • Koegl F, Toennis B., 1936. Uber das bios-problem: Darstellung von krystallisiertem Biotin aus eigelb. Z. Physiol. Chem. 242: 43-73.
    • (1936) Z. Physiol. Chem. , vol.242 , pp. 43-73
    • Koegl, F.1    Toennis, B.2
  • 36
    • 0036129945 scopus 로고    scopus 로고
    • Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site
    • DOI 10.1110/ps.4150102
    • Korndorfer IP, Skerra A., 2002. Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site. Protein Sci. 11: 883-893. (Pubitemid 34241296)
    • (2002) Protein Science , vol.11 , Issue.4 , pp. 883-893
    • Korndorfer, I.P.1    Skerra, A.2
  • 37
    • 0021194407 scopus 로고
    • Avidin, a high affinity biotin-binding protein, as a tool and subject of biological research
    • Korpela J., 1984. Avidin, a high affinity biotin-binding protein, as a tool and subject of biological research. Med. Biol. 62: 5-26. (Pubitemid 14058822)
    • (1984) Medical Biology , vol.62 , Issue.1 , pp. 5-26
    • Korpela, J.1
  • 38
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ., 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 39
    • 33645889302 scopus 로고    scopus 로고
    • The discovery of avidin by Esmond E. Snell
    • Kresge N., 2004. The discovery of avidin by Esmond E. Snell. J. Biol. Chem. 279: e5.
    • (2004) J. Biol. Chem. , vol.279
    • Kresge, N.1
  • 40
    • 0032704893 scopus 로고    scopus 로고
    • Mutation of a critical tryptophan to lysine in avidin or streptavidin may explain why sea urchin fibropellin adopts an avidin-like domain
    • DOI 10.1016/S0014-5793(99)01423-4, PII S0014579399014234
    • Laitinen OH, Airenne KJ, Marttila AT, Kulik T, Porkka E, Bayer EA, Wilchek M, Kulomaa MS., 1999. Mutation of a critical tryptophan to lysine in avidin or streptavidin may explain why sea urchin fibropellin adopts an avidin-like domain. FEBS Lett. 461: 52-58. (Pubitemid 29528569)
    • (1999) FEBS Letters , vol.461 , Issue.1-2 , pp. 52-58
    • Laitinen, O.H.1    Airenne, K.J.2    Marttila, A.T.3    Kulik, T.4    Porkka, E.5    Bayer, E.A.6    Wilchek, M.7    Kulomaa, M.S.8
  • 41
    • 4544375452 scopus 로고    scopus 로고
    • The biotin connection
    • Lane MD., 2004. The biotin connection. J. Biol. Chem. 279.
    • (2004) J. Biol. Chem. , pp. 279
    • Lane, M.D.1
  • 42
    • 0028381539 scopus 로고
    • Sensing discrete streptavidin-biotin interactions with atomic force microscopy
    • Lee GU, Kidwell DA, Colton RJ., 1994. Sensing discrete streptavidin-biotin interactions with atomic force microscopy. Langmuir 10: 354-357.
    • (1994) Langmuir , vol.10 , pp. 354-357
    • Lee, G.U.1    Kidwell, D.A.2    Colton, R.J.3
  • 43
    • 24344508229 scopus 로고    scopus 로고
    • Specific molecular interactions by force spectroscopy: From single bonds to collective properties
    • DOI 10.1016/j.bpc.2005.03.013, PII S030146220500089X
    • Levy R, Maaloum M., 2005. Specific molecular interactions by force spectroscopy: from single bonds to collective properties. Biophys. Chem. 117: 233-237. (Pubitemid 41253598)
    • (2005) Biophysical Chemistry , vol.117 , Issue.3 , pp. 233-237
    • Levy, R.1    Maaloum, M.2
  • 44
    • 77954803840 scopus 로고    scopus 로고
    • Apparent dependence of rupture force on loading rate in single-molecule force spectroscopy
    • Li N, Guo S, Akhremitchev BB., 2010. Apparent dependence of rupture force on loading rate in single-molecule force spectroscopy. Chemphyschem 11: 2096-2098.
    • (2010) Chemphyschem , vol.11 , pp. 2096-2098
    • Li, N.1    Guo, S.2    Akhremitchev, B.B.3
  • 46
    • 0033077975 scopus 로고    scopus 로고
    • Specific interactions between biotin and avidin studied by atomic force microscopy using the Poisson statistical analysis method
    • Lo Y-S, Huefner ND, Chan WS, Stevens F, Harris JM, Beebe TP., 1999. Specific interactions between biotin and avidin studied by atomic force microscopy using the Poisson statistical analysis method. Langmuir 15: 1373-1382.
    • (1999) Langmuir , vol.15 , pp. 1373-1382
    • Lo, Y.-S.1    Huefner, N.D.2    Chan, W.S.3    Stevens, F.4    Harris, J.M.5    Beebe, T.P.6
  • 47
    • 0037067292 scopus 로고    scopus 로고
    • Loading-rate dependence of individual ligand-receptor bond-rupture forces studied by atomic force microscopy
    • DOI 10.1021/la001569g
    • Lo Y-S, Zhu Y-J, Beebe TP., 2001. Loading-rate dependence of individual ligand-receptor bond-rupture forces studied by atomic force microscopy. Langmuir 17: 3741-3748. (Pubitemid 35330409)
    • (2001) Langmuir , vol.17 , Issue.12 , pp. 3741-3748
    • Lo, Y.-S.1    Zhu, Y.-J.2    Beebe Jr., T.P.3
  • 48
    • 21244479320 scopus 로고    scopus 로고
    • Force history dependence of receptor-ligand dissociation
    • DOI 10.1529/biophysj.104.050567
    • Marshall BT, Sarangapani KK, Lou J, McEver RP, Zhu C., 2005. Force history dependence of receptor-ligand dissociation. Biophys. J. 88: 1458-1466. (Pubitemid 40975972)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 1458-1466
    • Marshall, B.T.1    Sarangapani, K.K.2    Lou, J.3    McEver, R.P.4    Zhu, C.5
  • 49
    • 0000138158 scopus 로고
    • Avidin. 2. Purification and composition
    • Melamed MD, Green NM., 1963. Avidin. 2. Purification and composition. Biochem. J. 89: 591-599.
    • (1963) Biochem. J. , vol.89 , pp. 591-599
    • Melamed, M.D.1    Green, N.M.2
  • 50
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • DOI 10.1038/16219
    • Merkel R, Nassoy P, Leung A, Ritchie K, Evans E., 1999. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 397: 50-53. (Pubitemid 29038244)
    • (1999) Nature , vol.397 , Issue.6714 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 51
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic Molecular Graphics
    • DOI 10.1016/S0076-6879(97)77028-9
    • Merritt EA, Bacon DJ., 1997. Raster3D: photorealistic molecular graphics. Meth. Enzymol. 277: 505-524. (Pubitemid 27390937)
    • (1997) Methods in Enzymology , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 52
    • 0028140707 scopus 로고
    • Intermolecular forces and energies between ligands and receptors
    • Moy VT, Florin EL, Gaub HE., 1994a. Intermolecular forces and energies between ligands and receptors. Science 266: 257-259. (Pubitemid 24343509)
    • (1994) Science , vol.266 , Issue.5183 , pp. 257-259
    • Moy, V.T.1    Florin, E.-L.2    Gaub, H.E.3
  • 53
    • 0028766095 scopus 로고
    • Adhesive forces between ligand and receptor measured by AFM
    • Moy VT, Florin EL, Gaub HE., 1994b. Adhesive forces between ligand and receptor measured by AFM. Colloids Surf. A 93: 343-348.
    • (1994) Colloids Surf. A , vol.93 , pp. 343-348
    • Moy, V.T.1    Florin, E.L.2    Gaub, H.E.3
  • 54
    • 30644476474 scopus 로고    scopus 로고
    • Dynamic force spectroscopy of the digoxigenin-antibody complex
    • DOI 10.1016/j.febslet.2005.12.052, PII S0014579305015358
    • Neuert G, Albrecht C, Pamir E, Gaub HE., 2006. Dynamic force spectroscopy of the digoxigenin-antibody complex. FEBS Lett. 580: 505-509. (Pubitemid 43089679)
    • (2006) FEBS Letters , vol.580 , Issue.2 , pp. 505-509
    • Neuert, G.1    Albrecht, C.2    Pamir, E.3    Gaub, H.E.4
  • 55
    • 34447314421 scopus 로고    scopus 로고
    • An integrated methodology for data processing in dynamic force spectroscopy of ligand-receptor binding
    • DOI 10.1016/j.ultramic.2007.04.019, PII S0304399107001003
    • Odorico M, Teulon J-M, Berthoumieu O, Chen SWW, Parot P, Pellequer J-L., 2007a. An integrated methodology for data processing in Dynamic Force Spectroscopy of ligand-receptor binding. Ultramicroscopy 107: 887-894. (Pubitemid 47095097)
    • (2007) Ultramicroscopy , vol.107 , Issue.10-11 , pp. 887-894
    • Odorico, M.1    Teulon, J.-M.2    Berthoumieu, O.3    Chen, S.-w.W.4    Parot, P.5    Pellequer, J.-L.6
  • 57
    • 28444492383 scopus 로고    scopus 로고
    • The solution to the streptavidin-biotin paradox: The influence of history on the strength of single molecular bonds
    • DOI 10.1529/biophysj.105.067769
    • Pincet F, Husson J., 2005. The solution to the streptavidin-biotin paradox: the influence of history on the strength of single molecular bonds. Biophys. J. 89: 4374-4381. (Pubitemid 41725655)
    • (2005) Biophysical Journal , vol.89 , Issue.6 , pp. 4374-4381
    • Pincet, F.1    Husson, J.2
  • 58
    • 0025103931 scopus 로고
    • Dissociation rate constant of the biotin-streptavidin complex
    • DOI 10.1016/0022-1759(90)90328-S
    • Piran U, Riordan WJ., 1990. Dissociation rate constant of the biotin-streptavidin complex. J. Immunol. Methods 133: 141-143. (Pubitemid 20334494)
    • (1990) Journal of Immunological Methods , vol.133 , Issue.1 , pp. 141-143
    • Piran, U.1    Riordan, W.J.2
  • 59
    • 0032076568 scopus 로고    scopus 로고
    • A trivalent system from vancomycin-D-Ala-D-Ala with higher affinity than avidin-biotin
    • DOI 10.1126/science.280.5364.708
    • Rao J, Lahiri J, Isaacs L, Weis RM, Whitesides GM., 1998. A trivalent system from vancomycin.D-ala-D-Ala with higher affinity than avidin.biotin. Science 280: 708-711. (Pubitemid 28243338)
    • (1998) Science , vol.280 , Issue.5364 , pp. 708-711
    • Rao, J.1    Lahiri, J.2    Isaacs, L.3    Weis, R.M.4    Whitesides, G.M.5
  • 60
    • 38349086420 scopus 로고    scopus 로고
    • Energy landscape roughness of the streptavidin-biotin interaction
    • Rico F, Moy VT., 2007. Energy landscape roughness of the streptavidin-biotin interaction. J. Mol. Recognit. 20: 495-501.
    • (2007) J. Mol. Recognit. , vol.20 , pp. 495-501
    • Rico, F.1    Moy, V.T.2
  • 62
    • 0033861876 scopus 로고    scopus 로고
    • Model energy landscapes and the force-induced dissociation of ligand-receptor bonds
    • Strunz T, Oroszlan K, Schumakovitch I, Guntherodt H, Hegner M., 2000. Model energy landscapes and the force-induced dissociation of ligand-receptor bonds. Biophys. J. 79: 1206-1212.
    • (2000) Biophys. J. , vol.79 , pp. 1206-1212
    • Strunz, T.1    Oroszlan, K.2    Schumakovitch, I.3    Guntherodt, H.4    Hegner, M.5
  • 64
    • 39749143144 scopus 로고    scopus 로고
    • Probing the interaction between p53 and the bacterial protein azurin by single molecule force spectroscopy
    • DOI 10.1002/jmr.869
    • Taranta M, Bizzarri AR, Cannistraro S., 2008. Probing the interaction between p53 and the bacterial protein azurin by single molecule force spectroscopy. J. Mol. Recognit. 21: 63-70. (Pubitemid 351300460)
    • (2008) Journal of Molecular Recognition , vol.21 , Issue.1 , pp. 63-70
    • Taranta, M.1    Bizzarri, A.R.2    Cannistraro, S.3
  • 66
    • 58149277384 scopus 로고    scopus 로고
    • Deciphering the energy landscape of the interaction uranyl-DCP with antibodies using dynamic force spectroscopy
    • Teulon J-M, Parot P, Odorico M, Pellequer J-L., 2008. Deciphering the energy landscape of the interaction uranyl-DCP with antibodies using dynamic force spectroscopy. Biophys. J. 95: L63-65.
    • (2008) Biophys. J. , vol.95
    • Teulon, J.-M.1    Parot, P.2    Odorico, M.3    Pellequer, J.-L.4
  • 67
    • 33751204127 scopus 로고    scopus 로고
    • Dynamic force spectroscopy on soft molecular systems: Improved analysis of unbinding spectra with varying linker compliance
    • DOI 10.1016/j.colsurfb.2006.08.015, PII S0927776506002694
    • Thormann E, Hansen PL, Simonsen AC, Mouritsen OG., 2006. Dynamic force spectroscopy on soft molecular systems: improved analysis of unbinding spectra with varying linker compliance. Colloids Surf. B Biointerfaces 53: 149-156. (Pubitemid 44791890)
    • (2006) Colloids and Surfaces B: Biointerfaces , vol.53 , Issue.2 , pp. 149-156
    • Thormann, E.1    Hansen, P.L.2    Simonsen, A.C.3    Mouritsen, O.G.4
  • 68
    • 0037058902 scopus 로고    scopus 로고
    • The effect of force on thermodynamics and kinetics of single molecule reactions
    • DOI 10.1016/S0301-4622(02)00177-1, PII S0301462202001771
    • Tinoco I Jr, Bustamante C., 2002. The effect of force on thermodynamics and kinetics of single molecule reactions. Biophys. Chem. 101-102: 513-533. (Pubitemid 35462069)
    • (2002) Biophysical Chemistry , vol.101-102 , pp. 513-533
    • Tinoco Jr., I.1    Bustamante, C.2
  • 69
    • 33847701706 scopus 로고    scopus 로고
    • Role of Multiple Bonds Between the Single Cell Adhesion Molecules, Nectin and Cadherin, Revealed by High Sensitive Force Measurements
    • DOI 10.1016/j.jmb.2006.12.022, PII S0022283606016974
    • Tsukasaki Y, Kitamura K, Shimizu K, Iwane AH, Takai Y, Yanagida T., 2007. Role of multiple bonds between the single cell adhesion molecules, nectin and cadherin, revealed by high sensitive force measurements. J. Mol. Biol. 367: 996-1006. (Pubitemid 46386064)
    • (2007) Journal of Molecular Biology , vol.367 , Issue.4 , pp. 996-1006
    • Tsukasaki, Y.1    Kitamura, K.2    Shimizu, K.3    Iwane, A.H.4    Takai, Y.5    Yanagida, T.6
  • 70
    • 41649121704 scopus 로고    scopus 로고
    • Extending Bell's model: How force transducer stiffness alters measured unbinding forces and kinetics of molecular complexes
    • Walton EB, Lee S, Van Vliet KJ., 2008. Extending Bell's model: how force transducer stiffness alters measured unbinding forces and kinetics of molecular complexes. Biophys. J. 94: 2621-2630.
    • (2008) Biophys. J. , vol.94 , pp. 2621-2630
    • Walton, E.B.1    Lee, S.2    Van Vliet, K.J.3
  • 71
    • 0024588901 scopus 로고
    • Structural origins of high-affinity biotin binding to streptavidin
    • Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR., 1989. Structural origins of high-affinity biotin binding to streptavidin. Science 243: 85-88. (Pubitemid 19027930)
    • (1989) Science , vol.243 , Issue.4887 , pp. 85-88
    • Weber, P.C.1    Ohlendorf, D.H.2    Wendoloski, J.J.3    Salemme, F.R.4
  • 72
    • 0025281379 scopus 로고
    • Introduction to avidin-biotin technology
    • DOI 10.1016/0076-6879(90)84256-G
    • Wilchek M, Bayer EA., 1990. Introduction to avidin-biotin technology. Methods Enzymol. 184: 5-13. (Pubitemid 20219728)
    • (1990) Methods in Enzymology , vol.184 , pp. 5-13
    • Wilchek, M.1    Bayer, E.A.2
  • 73
    • 0037420289 scopus 로고    scopus 로고
    • Analytical descriptions of dynamic force spectroscopy: Behaviour of multiple connections
    • DOI 10.1016/S0003-2670(02)01569-6
    • Williams PM., 2003. Analytical descriptions of dynamic force spectroscopy: behaviour of multiple connections. Anal. Chim. Acta 479: 107-115. (Pubitemid 36173938)
    • (2003) Analytica Chimica Acta , vol.479 , Issue.1 , pp. 107-115
    • Williams, P.M.1
  • 74
    • 0033621525 scopus 로고    scopus 로고
    • Direct force measurements of the streptavidin-biotin interaction
    • DOI 10.1016/S1050-3862(99)00035-2, PII S1050386299000352
    • Wong J, Chilkoti A, Moy VT., 1999. Direct force measurements of the streptavidin-biotin interaction. Biomol. Eng. 16: 45-55. (Pubitemid 30184838)
    • (1999) Biomolecular Engineering , vol.16 , Issue.1-4 , pp. 45-55
    • Wong, J.1    Chilkoti, A.2    Moy, V.T.3
  • 75
    • 0032474758 scopus 로고    scopus 로고
    • Covalently functionalized nanotubes as nanometresized probes in chemistry and biology
    • DOI 10.1038/27873
    • Wong SS, Joselevich E, Woolley AT, Cheung CL, Lieber CM., 1998. Covalently functionalized nanotubes as nanometer-sized probes in chemistry and biology. Nature 394: 52-55. (Pubitemid 28321797)
    • (1998) Nature , vol.394 , Issue.6688 , pp. 52-55
    • Wong, S.S.1    Joselevich, E.2    Woolley, A.T.3    Cheung, C.L.4    Lieber, C.M.5
  • 76
    • 0034702770 scopus 로고    scopus 로고
    • Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy
    • DOI 10.1021/bi992715o
    • Yuan C, Chen A, Kolb P, Moy VT., 2000. Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy. Biochemistry 39: 10219-10223. (Pubitemid 30663044)
    • (2000) Biochemistry , vol.39 , Issue.33 , pp. 10219-10223
    • Yuan, C.1    Chen, A.2    Kolb, P.3    Moy, V.T.4
  • 77
    • 0038354493 scopus 로고    scopus 로고
    • Cooperative adhesion of ligand-receptor bonds
    • DOI 10.1016/S0301-4622(02)00381-2
    • Zhang X, Moy VT., 2003. Cooperative adhesion of ligand-receptor bonds. Biophys. Chem. 104: 271-278. (Pubitemid 36794478)
    • (2003) Biophysical Chemistry , vol.104 , Issue.1 , pp. 271-278
    • Zhang, X.1    Moy, V.T.2
  • 78
    • 33748698955 scopus 로고    scopus 로고
    • Unbinding of the streptavidin-biotin complex by atomic force microscopy: A hybrid simulation study
    • Zhou J, Zhang L, Leng Y, Tsao HK, Sheng YJ, Jiang S., 2006. Unbinding of the streptavidin-biotin complex by atomic force microscopy: a hybrid simulation study. J. Chem. Phys. 125: 104905.
    • (2006) J. Chem. Phys. , vol.125 , pp. 104905
    • Zhou, J.1    Zhang, L.2    Leng, Y.3    Tsao, H.K.4    Sheng, Y.J.5    Jiang, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.