메뉴 건너뛰기




Volumn 94, Issue 7, 2008, Pages 2621-2630

Extending Bell's model: How force transducer stiffness alters measured unbinding forces and kinetics of molecular complexes

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN; MOLECULAR MOTOR; STREPTAVIDIN;

EID: 41649121704     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.114454     Document Type: Article
Times cited : (82)

References (64)
  • 2
    • 33745950622 scopus 로고    scopus 로고
    • Probing drug-cell interactions
    • Van Vliet, K. J., and P. Hinterdorfer. 2006. Probing drug-cell interactions. NanoToday. 1:18-25.
    • (2006) NanoToday , vol.1 , pp. 18-25
    • Van Vliet, K.J.1    Hinterdorfer, P.2
  • 3
    • 34249936024 scopus 로고    scopus 로고
    • Forces and bond dynamics in cell adhesion
    • Evans, E. A., and D. A. Calderwood. 2007. Forces and bond dynamics in cell adhesion. Science. 316:1148-1153.
    • (2007) Science , vol.316 , pp. 1148-1153
    • Evans, E.A.1    Calderwood, D.A.2
  • 4
    • 34249930159 scopus 로고    scopus 로고
    • Single-molecule experiments in vitro and in silico
    • Sotomayor, M., and K. Schulten. 2007. Single-molecule experiments in vitro and in silico. Science. 316:1144-1148.
    • (2007) Science , vol.316 , pp. 1144-1148
    • Sotomayor, M.1    Schulten, K.2
  • 5
    • 0029407434 scopus 로고
    • Molecular-origins of the slow streptavidin-biotin dissociation kinetics
    • Chilkoti, A., and P. S. Stayton. 1995. Molecular-origins of the slow streptavidin-biotin dissociation kinetics. J. Am. Chem. Soc. 117:10622-10628.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 10622-10628
    • Chilkoti, A.1    Stayton, P.S.2
  • 6
    • 0032793576 scopus 로고    scopus 로고
    • The free energies for mutating S27 and W79 to alanine in streptavidin and its biotin complex: The relative size of polar and nonpolar free energies on biotin binding
    • Dixon, R. W., and P. Kollman. 1999. The free energies for mutating S27 and W79 to alanine in streptavidin and its biotin complex: the relative size of polar and nonpolar free energies on biotin binding. Proteins. 36:471-473.
    • (1999) Proteins , vol.36 , pp. 471-473
    • Dixon, R.W.1    Kollman, P.2
  • 8
    • 0024653594 scopus 로고
    • Crystal-structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation
    • Hendrickson, W. A., A. Pahler, J. L. Smith, Y. Satow, E. A. Merritt, and R. P. Phizackerley. 1989. Crystal-structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation. Proc. Natl. Acad. Sci. USA. 86:2190-2194.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2190-2194
    • Hendrickson, W.A.1    Pahler, A.2    Smith, J.L.3    Satow, Y.4    Merritt, E.A.5    Phizackerley, R.P.6
  • 9
    • 0034044384 scopus 로고    scopus 로고
    • 45 plays an important role in managing both the equilibrium and transition state energetics of the streptavidin-biotin system
    • 45 plays an important role in managing both the equilibrium and transition state energetics of the streptavidin-biotin system. Protein Sci. 9:878-885.
    • (2000) Protein Sci , vol.9 , pp. 878-885
    • Hyre, D.E.1    Le Trong, I.2    Freitag, S.3    Stenkamp, R.E.4    Stayton, P.S.5
  • 11
    • 0032568575 scopus 로고    scopus 로고
    • Energetic roles of hydrogen bonds at the ureido oxygen binding pocket in the streptavidinbiotin complex
    • Klumb, L. A., V. Chu, and P. S. Stayton. 1998. Energetic roles of hydrogen bonds at the ureido oxygen binding pocket in the streptavidinbiotin complex. Biochemistry. 37:7657-7663.
    • (1998) Biochemistry , vol.37 , pp. 7657-7663
    • Klumb, L.A.1    Chu, V.2    Stayton, P.S.3
  • 13
    • 0024588901 scopus 로고
    • Structural origins of high-affinity biotin binding to streptavidin
    • Weber, P. C., D. H. Ohlendorf, J. J. Wendoloski, and F. R. Salemme. 1989. Structural origins of high-affinity biotin binding to streptavidin. Science. 243:85-88.
    • (1989) Science , vol.243 , pp. 85-88
    • Weber, P.C.1    Ohlendorf, D.H.2    Wendoloski, J.J.3    Salemme, F.R.4
  • 14
    • 0026606240 scopus 로고
    • Crystallographic and thermodynamic comparison of natural and synthetic ligands bound to streptavidin
    • Weber, P. C., J. J. Wendoloski, M. W. Pantoliano, and F. R. Salemme. 1992. Crystallographic and thermodynamic comparison of natural and synthetic ligands bound to streptavidin. J. Am. Chem. Soc. 114:3197-3200.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 3197-3200
    • Weber, P.C.1    Wendoloski, J.J.2    Pantoliano, M.W.3    Salemme, F.R.4
  • 15
    • 0035865410 scopus 로고    scopus 로고
    • Detection of biological toxins on an active electronic microchip
    • Ewalt, K. L., R. W. Haigis, R. Rooney, D. Ackley, and M. Krihak. 2001. Detection of biological toxins on an active electronic microchip. Anal. Biochem. 289:162-172.
    • (2001) Anal. Biochem , vol.289 , pp. 162-172
    • Ewalt, K.L.1    Haigis, R.W.2    Rooney, R.3    Ackley, D.4    Krihak, M.5
  • 16
    • 0033136645 scopus 로고    scopus 로고
    • Epidermal growth factor radiopharmaceuticals: In-111 chelation, conjugation to a blood-brain barrier delivery vector via a biotin-polyethylene linker, pharmacokinetics, and in vivo imaging of experimental brain tumors
    • Kurihara, A., Y. Deguchi, and W. M. Pardridge. 1999. Epidermal growth factor radiopharmaceuticals: in-111 chelation, conjugation to a blood-brain barrier delivery vector via a biotin-polyethylene linker, pharmacokinetics, and in vivo imaging of experimental brain tumors. Bioconjug. Chem. 10:502-511.
    • (1999) Bioconjug. Chem , vol.10 , pp. 502-511
    • Kurihara, A.1    Deguchi, Y.2    Pardridge, W.M.3
  • 17
    • 0031735660 scopus 로고    scopus 로고
    • Improving tumor targeting and decreasing normal tissue uptake by optimizing the stoichiometry of a two-step biotinylated-antibody/streptavidin-based targeting strategy: Studies in a nude mouse xenograft model
    • Maraveyas, A., G. Rowlinson-Busza, S. Murray, and A. A. Epenetos. 1998. Improving tumor targeting and decreasing normal tissue uptake by optimizing the stoichiometry of a two-step biotinylated-antibody/streptavidin-based targeting strategy: studies in a nude mouse xenograft model. Int. J. Cancer. 78:610-617.
    • (1998) Int. J. Cancer , vol.78 , pp. 610-617
    • Maraveyas, A.1    Rowlinson-Busza, G.2    Murray, S.3    Epenetos, A.A.4
  • 19
    • 0030078147 scopus 로고    scopus 로고
    • Galactose-modified streptavidin-GCLC antifibrin monoclonal antibody conjugates: Application for two-step thrombus embolus imaging
    • Rosebrough, S. F., and M. Hashmi. 1996. Galactose-modified streptavidin-GCLC antifibrin monoclonal antibody conjugates: application for two-step thrombus embolus imaging. J. Pharmacol. Exp. Ther. 276:770-775.
    • (1996) J. Pharmacol. Exp. Ther , vol.276 , pp. 770-775
    • Rosebrough, S.F.1    Hashmi, M.2
  • 20
    • 0032957192 scopus 로고    scopus 로고
    • Organ selective delivery using a tissue-directed streptavidin-biotin system: Targeting 5-fluorouridine via TNP-streptavidin
    • Schechter, B., L. M. Chen, R. Arnon, and M. Wilchek. 1999. Organ selective delivery using a tissue-directed streptavidin-biotin system: targeting 5-fluorouridine via TNP-streptavidin. J. Drug Target. 6:337-348.
    • (1999) J. Drug Target , vol.6 , pp. 337-348
    • Schechter, B.1    Chen, L.M.2    Arnon, R.3    Wilchek, M.4
  • 21
    • 0023876319 scopus 로고
    • The avidin biotin complex in bioanalytical applications
    • Wilchek, M., and E. A. Bayer. 1988. The avidin biotin complex in bioanalytical applications. Anal. Biochem. 171:1-32.
    • (1988) Anal. Biochem , vol.171 , pp. 1-32
    • Wilchek, M.1    Bayer, E.A.2
  • 22
    • 0029035433 scopus 로고
    • Improved targeting of radiolabeled streptavidin in tumors pretargeted with biotinylated monoclonal-antibodies through an avidin chase
    • Yao, Z. S., M. L. Zhang, H. Kobayashi, H. Sakahara, H. Nakada, I. Yamashina, and J. Konishi. 1995. Improved targeting of radiolabeled streptavidin in tumors pretargeted with biotinylated monoclonal-antibodies through an avidin chase. J. Nucl. Med. 36:837-841.
    • (1995) J. Nucl. Med , vol.36 , pp. 837-841
    • Yao, Z.S.1    Zhang, M.L.2    Kobayashi, H.3    Sakahara, H.4    Nakada, H.5    Yamashina, I.6    Konishi, J.7
  • 23
    • 0031973478 scopus 로고    scopus 로고
    • Effect of administration route and dose of streptavidin or biotin on the tumor uptake of radioactivity in intraperitoneal tumor with multistep targeting
    • Zhang, M. L., Z. S. Yao, H. Sakahara, T. Saga, Y. Nakamoto, N. Sato, S. J. Zhao, H. Nakada, I. Yamashina, and J. Konishi. 1998. Effect of administration route and dose of streptavidin or biotin on the tumor uptake of radioactivity in intraperitoneal tumor with multistep targeting. Nucl. Med. Biol. 25:101-105.
    • (1998) Nucl. Med. Biol , vol.25 , pp. 101-105
    • Zhang, M.L.1    Yao, Z.S.2    Sakahara, H.3    Saga, T.4    Nakamoto, Y.5    Sato, N.6    Zhao, S.J.7    Nakada, H.8    Yamashina, I.9    Konishi, J.10
  • 25
    • 28444492383 scopus 로고    scopus 로고
    • The solution to the streptavidin-biotin paradox: The influence of history on the strength of single molecular bonds
    • Pincet, F., and J. Husson. 2005. The solution to the streptavidin-biotin paradox: the influence of history on the strength of single molecular bonds. Biophys. J. 89:4374-4381.
    • (2005) Biophys. J , vol.89 , pp. 4374-4381
    • Pincet, F.1    Husson, J.2
  • 26
    • 23744447015 scopus 로고    scopus 로고
    • Rupture force measurement of biotin-streptavidin bonds using optical trapping
    • Ota, T., T. Sugiura, and S. Kawata. 2005. Rupture force measurement of biotin-streptavidin bonds using optical trapping. Appl. Phys. Lett. 87:043901.
    • (2005) Appl. Phys. Lett , vol.87 , pp. 043901
    • Ota, T.1    Sugiura, T.2    Kawata, S.3
  • 27
    • 0036107283 scopus 로고    scopus 로고
    • Dissecting streptavidin-biotin interaction with a laminar flow chamber
    • Pierres, A., D. Touchard, A.-M. Benoliel, and P. Bongrand. 2002. Dissecting streptavidin-biotin interaction with a laminar flow chamber. Biophys. J. 82:3214-3223.
    • (2002) Biophys. J , vol.82 , pp. 3214-3223
    • Pierres, A.1    Touchard, D.2    Benoliel, A.-M.3    Bongrand, P.4
  • 28
    • 24144476563 scopus 로고    scopus 로고
    • Measuring single-bond rupture forces using high electric fields in microfluidic channels and DNA oligomers as force tags
    • Breisch, S., J. Gonska, H. Deissler, and M. Stelzle. 2005. Measuring single-bond rupture forces using high electric fields in microfluidic channels and DNA oligomers as force tags. Biophys. J. 89:L19-L21.
    • (2005) Biophys. J , vol.89
    • Breisch, S.1    Gonska, J.2    Deissler, H.3    Stelzle, M.4
  • 29
    • 11144243158 scopus 로고    scopus 로고
    • Sensitive bond force measurements of ligand-receptor pairs with magnetic beads
    • Panhorst, M., P.-B. Kamp, G. Reiss, and H. Bruckl. 2005. Sensitive bond force measurements of ligand-receptor pairs with magnetic beads. Biosens. Bioelectron. 20:1685-1689.
    • (2005) Biosens. Bioelectron , vol.20 , pp. 1685-1689
    • Panhorst, M.1    Kamp, P.-B.2    Reiss, G.3    Bruckl, H.4
  • 30
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • Merkel, R., P. Nassoy, A. Leung, K. Ritchie, and E. Evans. 1999. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature. 397:50-53.
    • (1999) Nature , vol.397 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 31
    • 0038354493 scopus 로고    scopus 로고
    • Cooperative adhesion of ligand-receptor bonds
    • Zhang, X., and V. T. Moy. 2003. Cooperative adhesion of ligand-receptor bonds. Biophys. Chem. 104:271-278.
    • (2003) Biophys. Chem , vol.104 , pp. 271-278
    • Zhang, X.1    Moy, V.T.2
  • 32
    • 0034702770 scopus 로고    scopus 로고
    • Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy
    • Yuan, C., A. Chen, P. Kolb, and V. T. Moy. 2000. Energy landscape of streptavidin-biotin complexes measured by atomic force microscopy. Biochemistry. 39:10219-10223.
    • (2000) Biochemistry , vol.39 , pp. 10219-10223
    • Yuan, C.1    Chen, A.2    Kolb, P.3    Moy, V.T.4
  • 33
    • 0033621525 scopus 로고    scopus 로고
    • Direct force measurements of the streptavidin-biotin interaction
    • Wong, J., A. Chilkoti, and V. T. Moy. 1999. Direct force measurements of the streptavidin-biotin interaction. Biomol. Eng. 16:45-55.
    • (1999) Biomol. Eng , vol.16 , pp. 45-55
    • Wong, J.1    Chilkoti, A.2    Moy, V.T.3
  • 34
    • 0028140707 scopus 로고
    • Intermolecular forces and energies between ligands and receptors
    • Moy, V. T., E.-L. Florin, and H. E. Gaub. 1994. Intermolecular forces and energies between ligands and receptors. Science. 266:257-259.
    • (1994) Science , vol.266 , pp. 257-259
    • Moy, V.T.1    Florin, E.-L.2    Gaub, H.E.3
  • 35
    • 0037180006 scopus 로고    scopus 로고
    • Temperature dependence of the biotin-avidin bond-rupture force studied by atomic force microscopy
    • Lo, Y.-S., J. Simons, and T. P. Beebe. 2002. Temperature dependence of the biotin-avidin bond-rupture force studied by atomic force microscopy. J. Phys. Chem. B. 106:9847-9852.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 9847-9852
    • Lo, Y.-S.1    Simons, J.2    Beebe, T.P.3
  • 36
    • 0037067292 scopus 로고    scopus 로고
    • Loading-rate dependence of individual ligand-receptor bond-rupture forces studied by atomic force microscopy
    • Lo, Y.-S., Y.-J. Zhu, and T. P. Beebe. 2001. Loading-rate dependence of individual ligand-receptor bond-rupture forces studied by atomic force microscopy. Langmuir. 17:3741-3748.
    • (2001) Langmuir , vol.17 , pp. 3741-3748
    • Lo, Y.-S.1    Zhu, Y.-J.2    Beebe, T.P.3
  • 37
    • 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., N. D. Huefner, W. S. Chan, F. Stevens, J. M. Harris, and T. P. Beebe. 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
  • 38
    • 0028381539 scopus 로고
    • Sensing discrete streptavidin-biotin interactions with atomic force microscopy
    • Lee, G. U., D. A. Kidwell, and R. J. Colton. 1994. Sensing discrete streptavidin-biotin interactions with atomic force microscopy. Langmuir. 3:354-357.
    • (1994) Langmuir , vol.3 , pp. 354-357
    • Lee, G.U.1    Kidwell, D.A.2    Colton, R.J.3
  • 39
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin, E.-L., V. T. Moy, and H. E. Gaub. 1994. Adhesion forces between individual ligand-receptor pairs. Science. 264:415-417.
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.-L.1    Moy, V.T.2    Gaub, H.E.3
  • 40
    • 0030059225 scopus 로고    scopus 로고
    • Ligand binding: Molecular mechanics calculation of the streptavidin-biotin rupture force
    • Grubmüller, H., B. Heymann, and P. Tavan. 1996. Ligand binding: molecular mechanics calculation of the streptavidin-biotin rupture force. Science. 271:954-955.
    • (1996) Science , vol.271 , pp. 954-955
    • Grubmüller, H.1    Heymann, B.2    Tavan, P.3
  • 41
    • 0030987036 scopus 로고    scopus 로고
    • Molecular dynamics study of unbinding of the avidin-biotin complex
    • Izrailev, S., S. Stepaniants, M. Balsera, Y. Oona, and K. Schulten. 1997. Molecular dynamics study of unbinding of the avidin-biotin complex. Biophys. J. 72:1568-1581.
    • (1997) Biophys. J , vol.72 , pp. 1568-1581
    • Izrailev, S.1    Stepaniants, S.2    Balsera, M.3    Oona, Y.4    Schulten, K.5
  • 42
    • 34547397317 scopus 로고    scopus 로고
    • Chemomechanical mapping of ligand-receptor binding kinetics on cells
    • Lee, S., J. Mandic, and K. J. VanVliet. 2007. Chemomechanical mapping of ligand-receptor binding kinetics on cells. Proc. Natl. Acad. Sci. USA. 104:9609-9614.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 9609-9614
    • Lee, S.1    Mandic, J.2    VanVliet, K.J.3
  • 44
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell, G. I. 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
  • 45
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E., and K. Ritchie. 1997. Dynamic strength of molecular adhesion bonds. Biophys. J. 72:1541-1555.
    • (1997) Biophys. J , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 46
    • 0142029493 scopus 로고    scopus 로고
    • The biomechanics toolbox: Experimental approaches for living cells and biomolecules
    • VanVliet, K. J., G. Bao, and S. Suresh. 2003. The biomechanics toolbox: experimental approaches for living cells and biomolecules. Acta Mater. 51:5881-5905.
    • (2003) Acta Mater , vol.51 , pp. 5881-5905
    • VanVliet, K.J.1    Bao, G.2    Suresh, S.3
  • 47
    • 33845360436 scopus 로고    scopus 로고
    • Equilibration of experimentally determined protein structures for molecular dynamics simulation
    • Walton, E. B., and K. J. Van Vliet. 2006. Equilibration of experimentally determined protein structures for molecular dynamics simulation. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 74:061901.
    • (2006) Phys. Rev. E Stat. Nonlin. Soft Matter Phys , vol.74 , pp. 061901
    • Walton, E.B.1    Van Vliet, K.J.2
  • 48
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen, H., D. van der Spoel, and R. van Drunen. 1995. GROMACS: a message-passing parallel molecular dynamics implementation. Comput. Phys. Commun. 91:43-56.
    • (1995) Comput. Phys. Commun , vol.91 , pp. 43-56
    • Berendsen, H.1    van der Spoel, D.2    van Drunen, R.3
  • 49
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., B. Hess, and D. van der Spoel. 2001. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7:306-317.
    • (2001) J. Mol. Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 50
    • 0036371130 scopus 로고    scopus 로고
    • Single molecule force measurements
    • Chen, A., and V. T. Moy. 2000. Single molecule force measurements. Methods Cell Biol. 68:301-309.
    • (2000) Methods Cell Biol , vol.68 , pp. 301-309
    • Chen, A.1    Moy, V.T.2
  • 52
    • 36449007442 scopus 로고
    • Calibration of atomic-force microscope tips
    • Hutter, J. L., and J. Bechoefer. 1993. Calibration of atomic-force microscope tips. Rev. Sci. Instrum. 64:1868-1873.
    • (1993) Rev. Sci. Instrum , vol.64 , pp. 1868-1873
    • Hutter, J.L.1    Bechoefer, J.2
  • 53
    • 34347209835 scopus 로고
    • Calibration of thermal noise in atomic force microscopy
    • Butt, H. J., and M. Jaschke. 1995. Calibration of thermal noise in atomic force microscopy. Nanotechnology. 6:1-7.
    • (1995) Nanotechnology , vol.6 , pp. 1-7
    • Butt, H.J.1    Jaschke, M.2
  • 54
    • 13744260911 scopus 로고    scopus 로고
    • Hydrodynamic effects in fast AFM single-molecule force measurements
    • Janovjak, H., J. Struckmeier, and D. J. Muller. 2005. Hydrodynamic effects in fast AFM single-molecule force measurements. Eur. Biophys. J. 34:91-96.
    • (2005) Eur. Biophys. J , vol.34 , pp. 91-96
    • Janovjak, H.1    Struckmeier, J.2    Muller, D.J.3
  • 55
    • 0037022522 scopus 로고    scopus 로고
    • Correction of microrheological measurements of soft samples with atomic force microscopy for the hydrodynamic drag on the cantilever
    • Alcaraz, J., L. Buscemi, M. P. de Morales, J. Colchero, A. Baro, and D. Navajas. 2002. Correction of microrheological measurements of soft samples with atomic force microscopy for the hydrodynamic drag on the cantilever. Langmuir. 18:716-721.
    • (2002) Langmuir , vol.18 , pp. 716-721
    • Alcaraz, J.1    Buscemi, L.2    de Morales, M.P.3    Colchero, J.4    Baro, A.5    Navajas, D.6
  • 57
    • 30644476474 scopus 로고    scopus 로고
    • Dynamic force spectroscopy of the digoxigenin-antibody complex
    • Neuert, G., C. Albrecht, E. Pamir, and H. E. Gaub. 2006. Dynamic force spectroscopy of the digoxigenin-antibody complex. FEBS Lett. 580:505-509.
    • (2006) FEBS Lett , vol.580 , pp. 505-509
    • Neuert, G.1    Albrecht, C.2    Pamir, E.3    Gaub, H.E.4
  • 58
    • 0033552676 scopus 로고    scopus 로고
    • Looking inside molecular bonds at biological interfaces with dynamic force spectroscopy
    • Evans, E. 1999. Looking inside molecular bonds at biological interfaces with dynamic force spectroscopy. Biophys. Chem. 82:83-97.
    • (1999) Biophys. Chem , vol.82 , pp. 83-97
    • Evans, E.1
  • 59
    • 33646192682 scopus 로고    scopus 로고
    • A coarse-grained model for force-induced protein deformation and kinetics
    • Karcher, H., S. E. Lee, M. R. Kaazempur-Mofrad, and R. D. Kamm. 2006. A coarse-grained model for force-induced protein deformation and kinetics. Biophys. J. 90:2686-2697.
    • (2006) Biophys. J , vol.90 , pp. 2686-2697
    • Karcher, H.1    Lee, S.E.2    Kaazempur-Mofrad, M.R.3    Kamm, R.D.4
  • 60
    • 34247640029 scopus 로고    scopus 로고
    • Wen, J.-D., M. Manosas, P. T. X. Li, S. B. Smith, C. Bustamante, F. Ritort, and I. T. Jr. 2007. Force unfolding kinetics of RNA using optical tweezers. I. Effects of experimental variables on measured results. Biophys. J. 92:2996-3009.
    • Wen, J.-D., M. Manosas, P. T. X. Li, S. B. Smith, C. Bustamante, F. Ritort, and I. T. Jr. 2007. Force unfolding kinetics of RNA using optical tweezers. I. Effects of experimental variables on measured results. Biophys. J. 92:2996-3009.
  • 61
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force-lifetime and chemistry in single molecular bonds
    • Evans, E. 2001. Probing the relation between force-lifetime and chemistry in single molecular bonds. Annu. Rev. Biophys. Biomol. 30:105-128.
    • (2001) Annu. Rev. Biophys. Biomol , vol.30 , pp. 105-128
    • Evans, E.1
  • 62
    • 0025103931 scopus 로고
    • Dissociation rate constant of the biotin-streptavidin complex
    • Piran, U., and W. Riordan. 1990. Dissociation rate constant of the biotin-streptavidin complex. J. Immunol. Methods. 133:141-143.
    • (1990) J. Immunol. Methods , vol.133 , pp. 141-143
    • Piran, U.1    Riordan, W.2
  • 63
    • 0035824616 scopus 로고    scopus 로고
    • Development and characterization of a series of soluble tetrameric and monomeric streptavidin muteins with differential biotin binding affinities
    • Qureshi, M. H., J. C. Yeung, S.-C. Wu, and S.-L. Wong. 2001. Development and characterization of a series of soluble tetrameric and monomeric streptavidin muteins with differential biotin binding affinities. J. Biol. Chem. 276:46422-46428.
    • (2001) J. Biol. Chem , vol.276 , pp. 46422-46428
    • Qureshi, M.H.1    Yeung, J.C.2    Wu, S.-C.3    Wong, S.-L.4
  • 64
    • 14744281200 scopus 로고    scopus 로고
    • Growth and shape stability of a biological membrane adhesion complex in the diffusion-mediated regime
    • Shenoy, V. B., and L. B. Freund. 2005. Growth and shape stability of a biological membrane adhesion complex in the diffusion-mediated regime. Proc. Natl. Acad. Sci. USA. 102:3213-3218.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3213-3218
    • Shenoy, V.B.1    Freund, L.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.