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Volumn 83, Issue 4, 2002, Pages 2211-2218

Plastic deformation of protein monolayers

Author keywords

[No Author keywords available]

Indexed keywords

GLOBULAR PROTEIN;

EID: 0036789732     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(02)73981-7     Document Type: Article
Times cited : (14)

References (37)
  • 3
    • 0000030050 scopus 로고
    • Activation energy spectrum of a biomolecule: Photodissociation of carbonmonoxy myoglobin at low temperatures
    • Austin, R. H., K. Beeson, L. Eisenstein, H. Faruenfelder, I. C. Gunsalus, and V. P. Marshall. 1974. Activation energy spectrum of a biomolecule: Photodissociation of carbonmonoxy myoglobin at low temperatures. Phys. Rev. Lett. 32:403.
    • (1974) Phys. Rev. Lett. , vol.32 , pp. 403
    • Austin, R.H.1    Beeson, K.2    Eisenstein, L.3    Faruenfelder, H.4    Gunsalus, I.C.5    Marshall, V.P.6
  • 4
    • 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
  • 5
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best, R. B., B. Li, A. Steward, V. Dagget, and J. Clarke. 2001. Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys. J. 81: 2344-2356.
    • (2001) Biophys. J. , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Dagget, V.4    Clarke, J.5
  • 6
    • 0030588310 scopus 로고    scopus 로고
    • Multiple alternating molecular layers of albumin and heparin on solid surfaces
    • Brynda, E., and M. Houska. 1996. Multiple alternating molecular layers of albumin and heparin on solid surfaces. J. Colloid Int. Sci. 183:18-25.
    • (1996) J. Colloid Int. Sci. , vol.183 , pp. 18-25
    • Brynda, E.1    Houska, M.2
  • 8
    • 0025179832 scopus 로고
    • Protein folding
    • Creighton, T. E. 1990. Protein folding. Biochem. J. 270:1-16.
    • (1990) Biochem. J. , vol.270 , pp. 1-16
    • Creighton, T.E.1
  • 9
    • 0023140044 scopus 로고
    • Multiple conformational states of proteins-a molecular dynamics analysis of myoglobin
    • Elber, R., and M. Karplus. 1987. Multiple conformational states of proteins-a molecular dynamics analysis of myoglobin. Science. 235:318.
    • (1987) Science , vol.235 , pp. 318
    • Elber, R.1    Karplus, M.2
  • 10
    • 0029664490 scopus 로고    scopus 로고
    • 2 and glass surfaces with ultrathin dextran films and deposition of lipid bilayers
    • 2 and glass surfaces with ultrathin dextran films and deposition of lipid bilayers. Biosens. Bioelectron. 11:565-577.
    • (1996) Biosens. Bioelectron. , vol.11 , pp. 565-577
    • Elender, G.1    Kuhner, M.2    Sackmann, E.3
  • 11
    • 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
  • 12
    • 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
  • 13
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., S. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 14
    • 0008884532 scopus 로고
    • Slow viscous motion of a sphere parallel to a plane wall. II. Couette flow
    • Goldman, A. J., R. G. Cox, and H. Brenner. 1967. Slow viscous motion of a sphere parallel to a plane wall. II. Couette flow. Chem. Eng. Sci. 22:653-660.
    • (1967) Chem. Eng. Sci. , vol.22 , pp. 653-660
    • Goldman, A.J.1    Cox, R.G.2    Brenner, H.3
  • 15
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He, X. M., and D. C. Carter. 1992. Atomic structure and chemistry of human serum albumin. Nature. 358:209.
    • (1992) Nature , vol.358 , pp. 209
    • He, X.M.1    Carter, D.C.2
  • 19
    • 0001686896 scopus 로고    scopus 로고
    • Measuring the spring constant of a single polymer chain
    • Jensenius, H., and G. Zocchi. 1997. Measuring the spring constant of a single polymer chain. Phys. Rev. Lett. 79:5030-5033.
    • (1997) Phys. Rev. Lett. , vol.79 , pp. 5030-5033
    • Jensenius, H.1    Zocchi, G.2
  • 20
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer, M. S. Z., S. B. Smith, H. L. Granzier, and C. Bustamante. 1997. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science. 276:1112-1115.
    • (1997) Science , vol.276 , pp. 1112-1115
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 21
    • 0000324979 scopus 로고    scopus 로고
    • Ultrathin hydrated dextran films grafted on glass: Preparation and characterization of structural, viscous, and elastic properties by quantitative microinterferometry
    • Kuhner, M., and E. Sackmann. 1996. Ultrathin hydrated dextran films grafted on glass: preparation and characterization of structural, viscous, and elastic properties by quantitative microinterferometry. Langmuir. 12:4866-4876.
    • (1996) Langmuir , vol.12 , pp. 4866-4876
    • Kuhner, M.1    Sackmann, E.2
  • 22
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • Merkel, R. P., A. L. Nassoy, 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.P.1    Nassoy, A.L.2    Ritchie, K.3    Evans, E.4
  • 23
    • 0010559962 scopus 로고
    • The slow stretch in indiarubber, glass, and metal wires when subjected to a constant pull
    • Phillips, F. P. 1905. The slow stretch in indiarubber, glass, and metal wires when subjected to a constant pull. Phil. Mag. 9:513.
    • (1905) Phil. Mag. , vol.9 , pp. 513
    • Phillips, F.P.1
  • 24
    • 0025384433 scopus 로고
    • Total internal reflection microscopy: A quantitative tool for the measurement of colloidal forces
    • Prieve, D. C., and N. A. Frej. 1990. Total internal reflection microscopy: a quantitative tool for the measurement of colloidal forces. Langmuir. 6:396-403.
    • (1990) Langmuir , vol.6 , pp. 396-403
    • Prieve, D.C.1    Frej, N.A.2
  • 25
    • 0027562182 scopus 로고
    • Scattering of an evanescent surface wave by a microscopic dielectric sphere
    • Prieve, D. C., and J. Y. Walz. 1993. Scattering of an evanescent surface wave by a microscopic dielectric sphere. Appl. Opt. 32:1629-1641.
    • (1993) Appl. Opt. , vol.32 , pp. 1629-1641
    • Prieve, D.C.1    Walz, J.Y.2
  • 26
    • 0002693020 scopus 로고
    • Physical basis of the stability of the folded conformatioins of proteins
    • T. E. Creighton, editor. Freeman and Co., New York
    • Privalov, P. L. 1992. Physical basis of the stability of the folded conformatioins of proteins. In Protein Folding. T. E. Creighton, editor. Freeman and Co., New York. 83-126.
    • (1992) Protein Folding , pp. 83-126
    • Privalov, P.L.1
  • 27
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 28
    • 0017528462 scopus 로고
    • Viscoelastic properties of very dilute paramyosin solutions
    • Rosser, R. W., J. L. Schrag, J. D. Ferry, and M. Greaser. 1977. Viscoelastic properties of very dilute paramyosin solutions. Macromolecules. 10: 978-980.
    • (1977) Macromolecules , vol.10 , pp. 978-980
    • Rosser, R.W.1    Schrag, J.L.2    Ferry, J.D.3    Greaser, M.4
  • 29
    • 0033050306 scopus 로고    scopus 로고
    • 2-integrins, and CD45 to neutrophil cytoskeleton and membrane
    • 2-integrins, and CD45 to neutrophil cytoskeleton and membrane. Biophys. J. 77:587-596.
    • (1999) Biophys. J. , vol.77 , pp. 587-596
    • Shao, J.-Y.1    Hochmuth, R.M.2
  • 30
    • 0033535939 scopus 로고    scopus 로고
    • Osmotic pressure contribution of albumin to colloidal interactions
    • Singh-Zocchi, M., A. Andreasen, and G. Zocchi. 1999. Osmotic pressure contribution of albumin to colloidal interactions. Proc. Natl. Acad. Sci. U.S.A. 96:6711-6715.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6711-6715
    • Singh-Zocchi, M.1    Andreasen, A.2    Zocchi, G.3
  • 32
    • 0027517403 scopus 로고
    • Adiabatic compressibility of myosin subfragment-1 and heavy meromyosin with or without nucleotide
    • Tamura, Y., N. Suzuki, and K. Mihashi. 1993. Adiabatic compressibility of myosin subfragment-1 and heavy meromyosin with or without nucleotide. Biophys. J. 65:1899-1905.
    • (1993) Biophys. J. , vol.65 , pp. 1899-1905
    • Tamura, Y.1    Suzuki, N.2    Mihashi, K.3
  • 33
    • 0031910473 scopus 로고    scopus 로고
    • Effect of substrate roughness on D spacing supports theoretical resolution of vapor pressure paradox
    • Tristram-Nagle, S., H. I. Petrache, R. M. Suter, and J. F. Nagle. 1998. Effect of substrate roughness on D spacing supports theoretical resolution of vapor pressure paradox. Biophys. J. 74:1421-1427.
    • (1998) Biophys. J. , vol.74 , pp. 1421-1427
    • Tristram-Nagle, S.1    Petrache, H.I.2    Suter, R.M.3    Nagle, J.F.4
  • 34
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • Tskhovrebova, L., J. Trinick, J. A. Sleep, and R. M. Simmons. 1997. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature. 387:308-312.
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 35
    • 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
  • 36
  • 37
    • 0034764282 scopus 로고    scopus 로고
    • Force measurements on single molecular contacts through evanescent wave microscopy
    • Zocchi, G. 2001. Force measurements on single molecular contacts through evanescent wave microscopy. Biophys. J. 81:2946-2953.
    • (2001) Biophys. J. , vol.81 , pp. 2946-2953
    • Zocchi, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.