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Volumn 94, Issue 1, 2008, Pages 79-89

How a vicinal layer of solvent modulates the dynamics of proteins

Author keywords

[No Author keywords available]

Indexed keywords

GLYCEROL; SOLVENT; WATER;

EID: 37749048444     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.116426     Document Type: Article
Times cited : (11)

References (44)
  • 1
    • 0037133221 scopus 로고    scopus 로고
    • Proteins: Paradigms of complexity
    • Frauenfelder, H. 2002. Proteins: paradigms of complexity. Proc. Natl. Acad. Sci. USA. 99:2479-2480.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2479-2480
    • Frauenfelder, H.1
  • 2
    • 5144223810 scopus 로고    scopus 로고
    • Bulk solvent and hydration-shell fluctuations, similar to alphaand beta-fluctuations in glasses, control protein motions and functions
    • Fenimore, P. W., H. Frauenfelder, B. H. McMahon, and R. D. Young. 2004. Bulk solvent and hydration-shell fluctuations, similar to alphaand beta-fluctuations in glasses, control protein motions and functions. Proc. Natl. Acad. Sci. USA. 101:14408-14413.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14408-14413
    • Fenimore, P.W.1    Frauenfelder, H.2    McMahon, B.H.3    Young, R.D.4
  • 4
    • 19044399611 scopus 로고    scopus 로고
    • Role of protein-water hydrogen bond dynamics in the protein dynamical transition
    • Tarek, M., and D. J. Tobias. 2002. Role of protein-water hydrogen bond dynamics in the protein dynamical transition. Phys. Rev. Lett. 88:138101.
    • (2002) Phys. Rev. Lett , vol.88 , pp. 138101
    • Tarek, M.1    Tobias, D.J.2
  • 5
    • 0034595671 scopus 로고    scopus 로고
    • How soft is a protein? A protein dynamics force constant measured by neutron scattering
    • Zaccai, G. 2000. How soft is a protein? A protein dynamics force constant measured by neutron scattering. Science. 288:1604-1607.
    • (2000) Science , vol.288 , pp. 1604-1607
    • Zaccai, G.1
  • 6
    • 18644379953 scopus 로고    scopus 로고
    • Coupling between lyzosyme and glycerol dynamics: Microscopic insights from molecular-dynamics simulations
    • Dirama, T. E., G. A. Carri, and A. P. Sokolov. 2005. Coupling between lyzosyme and glycerol dynamics: microscopic insights from molecular-dynamics simulations. J. Chem. Phys. 122:244910.
    • (2005) J. Chem. Phys , vol.122 , pp. 244910
    • Dirama, T.E.1    Carri, G.A.2    Sokolov, A.P.3
  • 7
    • 31144460588 scopus 로고    scopus 로고
    • Coupling between lyzosyme and trehalose dynamics: Microscopic insights from molecular-dynamics simulations
    • Dirama, T. E., J. E. Curtis, G.A. Carri, and A. P. Sokolov. 2006. Coupling between lyzosyme and trehalose dynamics: microscopic insights from molecular-dynamics simulations. J. Chem. Phys. 124:034901.
    • (2006) J. Chem. Phys , vol.124 , pp. 034901
    • Dirama, T.E.1    Curtis, J.E.2    Carri, G.A.3    Sokolov, A.P.4
  • 8
    • 33745788582 scopus 로고    scopus 로고
    • Controlling the protein dynamical transition with sugar-based bioprotectant matrices: A neutron scattering study
    • Cornicchi, E., M. Marconi, G. Onori, and A. Paciaroni. 2006. Controlling the protein dynamical transition with sugar-based bioprotectant matrices: a neutron scattering study. Biophys. J. 91:289-297.
    • (2006) Biophys. J , vol.91 , pp. 289-297
    • Cornicchi, E.1    Marconi, M.2    Onori, G.3    Paciaroni, A.4
  • 9
    • 0035997075 scopus 로고    scopus 로고
    • Effect of environment on the protein dynamical transition: A neutron scattering study
    • Paciaroni, A., S. Cinelli, and G. Onori. 2002. Effect of environment on the protein dynamical transition: a neutron scattering study. Biophys. J. 83:1157-1164.
    • (2002) Biophys. J , vol.83 , pp. 1157-1164
    • Paciaroni, A.1    Cinelli, S.2    Onori, G.3
  • 10
    • 0035996982 scopus 로고    scopus 로고
    • Relaxation kinetics and the glassiness of proteins: The case of bovine pancreatic trypsin inhibitor
    • Baysal, C., and A. R. Atilgan. 2002. Relaxation kinetics and the glassiness of proteins: the case of bovine pancreatic trypsin inhibitor. Biophys. J. 83:699-705.
    • (2002) Biophys. J , vol.83 , pp. 699-705
    • Baysal, C.1    Atilgan, A.R.2
  • 11
    • 21244471169 scopus 로고    scopus 로고
    • Relaxation kinetics and the glassiness of native proteins: Coupling of timescales
    • Baysal, C., and A. R. Atilgan. 2005. Relaxation kinetics and the glassiness of native proteins: coupling of timescales. Biophys. J. 88:1570-1576.
    • (2005) Biophys. J , vol.88 , pp. 1570-1576
    • Baysal, C.1    Atilgan, A.R.2
  • 13
    • 0037019460 scopus 로고    scopus 로고
    • Molecular dynamics of water at the protein-solvent interface
    • Bizzarri, A. R., and S. Cannistraro. 2002. Molecular dynamics of water at the protein-solvent interface. J. Phys. Chem. B. 106:6617-6633.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 6617-6633
    • Bizzarri, A.R.1    Cannistraro, S.2
  • 14
    • 0022762471 scopus 로고
    • Thermal properties of water in myoglobin crystals and solutions at subzero temperatures
    • Doster, W., A. Bachleitner, R. Dunau, M. Hiebl, and E. Loscher. 1986. Thermal properties of water in myoglobin crystals and solutions at subzero temperatures. Biophys. J. 50:213-219.
    • (1986) Biophys. J , vol.50 , pp. 213-219
    • Doster, W.1    Bachleitner, A.2    Dunau, R.3    Hiebl, M.4    Loscher, E.5
  • 15
    • 0030853055 scopus 로고    scopus 로고
    • The lubricant of life: A proposal that solvent water promotes extremely fast conformational fluctuations in mobile heteropolypeptide structure
    • Barron, L. D., L. Hecht, and G. Wilson. 1997. The lubricant of life: a proposal that solvent water promotes extremely fast conformational fluctuations in mobile heteropolypeptide structure. Biochemistry. 36:13143-13147.
    • (1997) Biochemistry , vol.36 , pp. 13143-13147
    • Barron, L.D.1    Hecht, L.2    Wilson, G.3
  • 16
    • 0037133342 scopus 로고    scopus 로고
    • Biological water at the protein surface: Dynamical solvation probed directly with femtosecond resolution
    • Pal, S. K., J. Peon, and A. H. Zewail. 2002. Biological water at the protein surface: dynamical solvation probed directly with femtosecond resolution. Proc. Natl. Acad. Sci. USA. 99:1763-1768.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1763-1768
    • Pal, S.K.1    Peon, J.2    Zewail, A.H.3
  • 17
    • 85035242434 scopus 로고    scopus 로고
    • Structure, dynamics, and energetics of water at the surface of a small globular protein: A molecular dynamics simulation
    • Dastidar, S. G., and C. Mukhopadhyay. 2003. Structure, dynamics, and energetics of water at the surface of a small globular protein: a molecular dynamics simulation. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 68:021921.
    • (2003) Phys. Rev. E Stat. Nonlin. Soft Matter Phys , vol.68 , pp. 021921
    • Dastidar, S.G.1    Mukhopadhyay, C.2
  • 19
    • 0029647450 scopus 로고
    • Protein reaction kinetics in a room-temperature glass
    • Hagen, S. J., and J. Hofrichter. 1995. Protein reaction kinetics in a room-temperature glass. Science. 269:959-962.
    • (1995) Science , vol.269 , pp. 959-962
    • Hagen, S.J.1    Hofrichter, J.2
  • 20
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • Ansari, A., C. M. Jones, E. R. Henry, J. Hofrichter, and W. A. Eaton. 1992. The role of solvent viscosity in the dynamics of protein conformational changes. Science. 256:1796-1798.
    • (1992) Science , vol.256 , pp. 1796-1798
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 22
    • 34447499925 scopus 로고    scopus 로고
    • Ligand recombination and a hierarchy of solvent slaved dynamics: The origin of kinetic phases in hemeproteins
    • Samuni, U., D. Dantsker, C. J. Roche, and J. M. Friedman. 2007. Ligand recombination and a hierarchy of solvent slaved dynamics: the origin of kinetic phases in hemeproteins. Gene. 398:234-248.
    • (2007) Gene , vol.398 , pp. 234-248
    • Samuni, U.1    Dantsker, D.2    Roche, C.J.3    Friedman, J.M.4
  • 27
    • 85031438501 scopus 로고    scopus 로고
    • Frisch, M. J., G. W. Trucks, H. B. Schlegel., G. E. Scuseria, M. A. Robb, J. R. Cheeseman, J. A. Montgomery Jr., T. Vreven, K. N. Kudin, J. C. Burant, J. M. Millam, S. S. Iyengar, J. Tomasi, et al. 2003. Gaussian 03. Gaussian, Pittsburgh PA.
    • Frisch, M. J., G. W. Trucks, H. B. Schlegel., G. E. Scuseria, M. A. Robb, J. R. Cheeseman, J. A. Montgomery Jr., T. Vreven, K. N. Kudin, J. C. Burant, J. M. Millam, S. S. Iyengar, J. Tomasi, et al. 2003. Gaussian 03. Gaussian, Pittsburgh PA.
  • 28
    • 0004249724 scopus 로고    scopus 로고
    • Accelrys, Inc, Accelrys, San Diego, CA
    • Accelrys, Inc. 2002. Materials Studio. Accelrys, San Diego, CA.
    • (2002) Materials Studio
  • 32
    • 0035118232 scopus 로고    scopus 로고
    • Protein flexibility from the dynamical transition: A force constant analysis
    • Bicout, D. J., and G. Zaccai. 2001. Protein flexibility from the dynamical transition: a force constant analysis. Biophys. J. 80:1115-1123.
    • (2001) Biophys. J , vol.80 , pp. 1115-1123
    • Bicout, D.J.1    Zaccai, G.2
  • 33
    • 0001421636 scopus 로고
    • Theorie des elektrischen Rückstandes in der Leidener Flasche. [in German]
    • Kohlrausch, R. 1974. Theorie des elektrischen Rückstandes in der Leidener Flasche. [in German]. Ann. Phys. Chem. (Leipzig). 91:179-214.
    • (1974) Ann. Phys. Chem. (Leipzig) , vol.91 , pp. 179-214
    • Kohlrausch, R.1
  • 34
    • 0014699523 scopus 로고
    • Non-symmetrical dielectric relaxation behavior arising from a simple empirical decay function
    • Williams, G., and D. C. Watts. 1970. Non-symmetrical dielectric relaxation behavior arising from a simple empirical decay function. Trans. Faraday Soc. 66:80-85.
    • (1970) Trans. Faraday Soc , vol.66 , pp. 80-85
    • Williams, G.1    Watts, D.C.2
  • 35
    • 0033918280 scopus 로고    scopus 로고
    • Single-particle tracking: Brownian dynamics of viscoelastic materials
    • Qian, H. 2000. Single-particle tracking: Brownian dynamics of viscoelastic materials. Biophys. J. 79:137-143.
    • (2000) Biophys. J , vol.79 , pp. 137-143
    • Qian, H.1
  • 36
    • 0037846499 scopus 로고    scopus 로고
    • Proteins as nano-machines: Dynamics-function relations studied by neutron scattering
    • Zaccai, G. 2003. Proteins as nano-machines: dynamics-function relations studied by neutron scattering. J. Phys. Condens. Matter. 15:S1673-S1682.
    • (2003) J. Phys. Condens. Matter , vol.15
    • Zaccai, G.1
  • 37
    • 0033613906 scopus 로고    scopus 로고
    • Native proteins are surface-molten solids: Application of the Lindemann criterion for the solid versus liquid state
    • Zhou, Y., D. Vitkup, and M. Karplus. 1999. Native proteins are surface-molten solids: application of the Lindemann criterion for the solid versus liquid state. J. Mol. Biol. 285:1371-1375.
    • (1999) J. Mol. Biol , vol.285 , pp. 1371-1375
    • Zhou, Y.1    Vitkup, D.2    Karplus, M.3
  • 39
    • 0033033595 scopus 로고    scopus 로고
    • Effect of glycerol on the interactions and solubility of bovine pancreatic trypsin inhibitor
    • Farnum, M., and C. Zukoski. 1999. Effect of glycerol on the interactions and solubility of bovine pancreatic trypsin inhibitor. Biophys. J. 76:2716-2726.
    • (1999) Biophys. J , vol.76 , pp. 2716-2726
    • Farnum, M.1    Zukoski, C.2
  • 40
    • 22544458487 scopus 로고    scopus 로고
    • Role of hydrogen bonds in the fast dynamics of binary glasses of trehalose and glycerol: A molecular dynamics simulation study
    • Dirama, T. E., G. A. Carri, and A. P. Sokolov. 2005. Role of hydrogen bonds in the fast dynamics of binary glasses of trehalose and glycerol: a molecular dynamics simulation study. J. Chem. Phys. 122:114505.
    • (2005) J. Chem. Phys , vol.122 , pp. 114505
    • Dirama, T.E.1    Carri, G.A.2    Sokolov, A.P.3
  • 41
    • 0030108972 scopus 로고    scopus 로고
    • Molecular dynamics analysis of coupling between librational motions and isomeric jumps in chain molecules
    • Baysal, C., A. R. Atilgan, B. Erman, and I. Bahar. 1996. Molecular dynamics analysis of coupling between librational motions and isomeric jumps in chain molecules. Macromolecules. 29:2510-2514.
    • (1996) Macromolecules , vol.29 , pp. 2510-2514
    • Baysal, C.1    Atilgan, A.R.2    Erman, B.3    Bahar, I.4
  • 42
    • 0028449730 scopus 로고
    • Contribution of short-range intramolecular interactions to local chain dynamics
    • Baysal, C., B. Erman, and I. Bahar. 1994. Contribution of short-range intramolecular interactions to local chain dynamics. Macromolecules. 27:3650-3657.
    • (1994) Macromolecules , vol.27 , pp. 3650-3657
    • Baysal, C.1    Erman, B.2    Bahar, I.3
  • 43
    • 0029699743 scopus 로고    scopus 로고
    • Molecular dynamics computer simulation of local dynamics in polyisoprene melts
    • Moe, N. E., and M. D. Ediger. 1996. Molecular dynamics computer simulation of local dynamics in polyisoprene melts. Polymer (Guildf.). 37:1787-1795.
    • (1996) Polymer (Guildf.) , vol.37 , pp. 1787-1795
    • Moe, N.E.1    Ediger, M.D.2
  • 44
    • 0030574936 scopus 로고    scopus 로고
    • Kinematics of polymer chains in dense medium. 4. Effect of backbone geometry and application to polybutadiene
    • Baysal, C., I. Bahar, B. Erman, and L. Monnerie. 1996. Kinematics of polymer chains in dense medium. 4. Effect of backbone geometry and application to polybutadiene. Macromolecules. 29:2980-2988.
    • (1996) Macromolecules , vol.29 , pp. 2980-2988
    • Baysal, C.1    Bahar, I.2    Erman, B.3    Monnerie, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.