메뉴 건너뛰기




Volumn 37, Issue 5, 2008, Pages 591-602

The dynamical transition of proteins, concepts and misconceptions

Author keywords

Dynamical transition; Glass transition; Lysozyme; Myoglobin; Neutron scattering; Protein dynamics; Protein hydration

Indexed keywords

METHYL GROUP;

EID: 45449115536     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-008-0274-3     Document Type: Article
Times cited : (162)

References (54)
  • 1
    • 0038732753 scopus 로고    scopus 로고
    • Energy resolution and dynamical heterogeneity effects on elastic incoherent neutron scattering from molecular systems
    • Becker T, Smith J (2003) Energy resolution and dynamical heterogeneity effects on elastic incoherent neutron scattering from molecular systems. Phys Rev E 67:021904-1-8
    • (2003) Phys Rev e , vol.67
    • Becker, T.1    Smith, J.2
  • 3
    • 0035118232 scopus 로고    scopus 로고
    • Protein flexibility from the dynamical transition, a force constant analyis
    • Bicout DJ, Zaccai G (2001) Protein flexibility from the dynamical transition, a force constant analyis. Biophys J 80:115-1123-8
    • (2001) Biophys J , vol.80 , pp. 115-11238
    • Bicout, D.J.1    Zaccai, G.2
  • 4
    • 84956237647 scopus 로고
    • A relation between fast and slow motions in glassy and liquid selenium
    • Buchenau U, Zorn R (1992) A relation between fast and slow motions in glassy and liquid selenium. Europhys Lett 18:523-528
    • (1992) Europhys Lett , vol.18 , pp. 523-528
    • Buchenau, U.1    Zorn, R.2
  • 5
    • 28844473534 scopus 로고    scopus 로고
    • Picosecond time scale fluctuations of proteins in glassy matrices: The role of viscosity
    • Cornicchi E, Onori G, Paciaroni A (2005) Picosecond time scale fluctuations of proteins in glassy matrices: the role of viscosity. Phys Rev Lett 95:158104-1-4
    • (2005) Phys Rev Lett , vol.95
    • Cornicchi, E.1    Onori, G.2    Paciaroni, A.3
  • 6
    • 0032863425 scopus 로고    scopus 로고
    • Enzyme dynamics and activity, the time scale dependence of dynamical transitions
    • Daniel RM, Finney JL, Reat V, Dunn R, Ferrand M, Smith J (1999) Enzyme dynamics and activity, the time scale dependence of dynamical transitions. Biophys J 77:2184-219
    • (1999) Biophys J , vol.77 , pp. 2184-219
    • Daniel, R.M.1    Finney, J.L.2    Reat, V.3    Dunn, R.4    Ferrand, M.5    Smith, J.6
  • 7
    • 0030771840 scopus 로고    scopus 로고
    • Vibrational frequencies as a probe of hydrogen bonds: Thermal expansion and glass transition of myoglobin in mixed solvents
    • Demmel F, Doster W, Petry W, Schulte A (1997) Vibrational frequencies as a probe of hydrogen bonds: thermal expansion and glass transition of myoglobin in mixed solvents. Eur Biophys J 26:327-335
    • (1997) Eur Biophys J , vol.26 , pp. 327-335
    • Demmel, F.1    Doster, W.2    Petry, W.3    Schulte, A.4
  • 8
    • 41649109124 scopus 로고    scopus 로고
    • Brownian oscillator analysis of molecular motions in biomolecules
    • Fitter J, Gutberlet T, Katsaras J (eds) Neutron scattering in biology.
    • Doster W (2005) Brownian oscillator analysis of molecular motions in biomolecules. In: Fitter J, Gutberlet T, Katsaras J (eds) Neutron scattering in biology. Springer series biological and medical physics, biomedical engineering, pp 461-482
    • (2005) Springer Series Biological and Medical Physics, Biomedical Engineering , pp. 461-482
    • Doster, W.1
  • 9
    • 33751226627 scopus 로고    scopus 로고
    • Dynamic structural distributions in proteins
    • Doster W (2006) Dynamic structural distributions in proteins. Physica B 385-386:831-834
    • (2006) Physica B , vol.385-386 , pp. 831-834
    • Doster, W.1
  • 11
    • 20144366574 scopus 로고    scopus 로고
    • Protein-water displacement distributions
    • Doster W, Settles M (2005) Protein-water displacement distributions. Biochim Biophys Act 1749:173-186
    • (2005) Biochim Biophys Act , vol.1749 , pp. 173-186
    • Doster, W.1    Settles, M.2
  • 12
    • 0022762471 scopus 로고
    • Thermal properties of water in myoglobin crystals and solutions at subzero temperatures
    • Doster W, Lüscher E, Bachleitner A, Dunau R, Hiebl M (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    Lüscher, E.2    Bachleitner, A.3    Dunau, R.4    Hiebl, M.5
  • 13
    • 0024976853 scopus 로고
    • Dynamical transition of myoglobin revealed by inelastic neutron scattering
    • Doster W, Cusack S, Petry W (1989) Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature 337:754-756
    • (1989) Nature , vol.337 , pp. 754-756
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 14
    • 45449116229 scopus 로고
    • Dynamic instability of liquid-like motions in proteins
    • Doster W, Cusack S, Petry W (1990) Dynamic instability of liquid-like motions in proteins. Phys Rev Lett 65:1083-1086
    • (1990) Phys Rev Lett , vol.65 , pp. 1083-1086
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 15
    • 0035398856 scopus 로고    scopus 로고
    • Elastic resolution spectroscopy: A method to study molecular motions in small biological samples
    • Doster W, Diehl M, Petry W, Ferrand M (2001) Elastic resolution spectroscopy: a method to study molecular motions in small biological samples. Physica B 301:65-68
    • (2001) Physica B , vol.301 , pp. 65-68
    • Doster, W.1    Diehl, M.2    Petry, W.3    Ferrand, M.4
  • 16
    • 0041766170 scopus 로고    scopus 로고
    • Time-of-flight elastic resolution spectroscopy: Time domain analysis of weakly scattering samples
    • Doster W, Diehl M, Gebhardt R, Lechner RE, Pieper J (2003) Time-of-flight elastic resolution spectroscopy: time domain analysis of weakly scattering samples. Chem Phys 292:487-494
    • (2003) Chem Phys , vol.292 , pp. 487-494
    • Doster, W.1    Diehl, M.2    Gebhardt, R.3    Lechner, R.E.4    Pieper, J.5
  • 18
    • 0027491027 scopus 로고
    • Thermal motions and function of bacteriorhodopsin in purple membranes: Effects of temperature and hydration studied by neutron scattering
    • Ferrand M, Dianoux AJ, Petry W, Zaccai G (1993) Thermal motions and function of bacteriorhodopsin in purple membranes: effects of temperature and hydration studied by neutron scattering. Proc Natl Acad Sci USA 90:9668-9672
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9668-9672
    • Ferrand, M.1    Dianoux, A.J.2    Petry, W.3    Zaccai, G.4
  • 19
    • 0030823236 scopus 로고    scopus 로고
    • Picosecond molecular motions in bacteriorhodopsin from neutron scattering
    • Fitter J, Lechner RE, Dencher NA (1997) Picosecond molecular motions in bacteriorhodopsin from neutron scattering. Biophys J 73:2126-2137
    • (1997) Biophys J , vol.73 , pp. 2126-2137
    • Fitter, J.1    Lechner, R.E.2    Dencher, N.A.3
  • 20
    • 13744256883 scopus 로고    scopus 로고
    • Protein dynamics in solution and powder measured by incoherent elastic neutron scattering
    • Gabel F (2005) Protein dynamics in solution and powder measured by incoherent elastic neutron scattering. Eur Biophys J 34:1-12
    • (2005) Eur Biophys J , vol.34 , pp. 1-12
    • Gabel, F.1
  • 22
    • 0004986545 scopus 로고    scopus 로고
    • Relaxation processes in supercooled liquids
    • Götze W, Sjögren L (2005) Relaxation processes in supercooled liquids. Rep Prog Phys 55:241-376
    • (2005) Rep Prog Phys , vol.55 , pp. 241-376
    • Götze, W.1    Sjögren, L.2
  • 23
    • 0041343122 scopus 로고    scopus 로고
    • Molecular dynamics decomposition of temperature-dependent elastic neutron scattering by a protein solution
    • Hayward JA, Finney JL, Daniel RM, Smith JC (2003) Molecular dynamics decomposition of temperature-dependent elastic neutron scattering by a protein solution. Biophys J 85:679-685
    • (2003) Biophys J , vol.85 , pp. 679-685
    • Hayward, J.A.1    Finney, J.L.2    Daniel, R.M.3    Smith, J.C.4
  • 24
    • 0002131341 scopus 로고
    • Evidence for conformational and diffusional mean square displacements in frozen aqueous solution of oxy-myoglobin
    • Keller H, Debrunner P (1980) Evidence for conformational and diffusional mean square displacements in frozen aqueous solution of oxy-myoglobin. Phys Rev Lett 45:68-71
    • (1980) Phys Rev Lett , vol.45 , pp. 68-71
    • Keller, H.1    Debrunner, P.2
  • 25
    • 0032512436 scopus 로고    scopus 로고
    • Solvent composition and viscosity effects on the kinetics of CO-binding to horse myoglobin
    • Kleinert Th, Doster W, Leyser H, Petry W, Schwarz V, Settles M (1998) Solvent composition and viscosity effects on the kinetics of CO-binding to horse myoglobin. Biochem 37:717-733
    • (1998) Biochem , vol.37 , pp. 717-733
    • Th, K.1    Doster, W.2    Leyser, H.3    Petry, W.4    Schwarz, V.5    Settles, M.6
  • 28
    • 2342427533 scopus 로고    scopus 로고
    • Mean square displacement relationship in bioprotectant systems by elastic neutron scattering
    • Magazu S, Maisano G, Migliardo F, Mondelli C (2004) Mean square displacement relationship in bioprotectant systems by elastic neutron scattering. Biophys J 86:3241-3249
    • (2004) Biophys J , vol.86 , pp. 3241-3249
    • Magazu, S.1    Maisano, G.2    Migliardo, F.3    Mondelli, C.4
  • 29
    • 21144437670 scopus 로고    scopus 로고
    • Protein dynamical heterogeneity derived from neutron incoherent elastic scattering
    • Nakagawa H, Kmikubo I, Kanaya T, Kataoka M (2004) Protein dynamical heterogeneity derived from neutron incoherent elastic scattering. J Phys Soc Jpn 73:491-495
    • (2004) J Phys Soc Jpn , vol.73 , pp. 491-495
    • Nakagawa, H.1    Kmikubo, I.2    Kanaya, T.3    Kataoka, M.4
  • 30
    • 33748623800 scopus 로고    scopus 로고
    • Conditioning action of the environment on the protein dynamics studied through elastic neutron scattering
    • 7
    • Paciaroni A, Cornicchi E, De Francesco A, Marconi M, Onori G (2006) Conditioning action of the environment on the protein dynamics studied through elastic neutron scattering. Eur Biophys J 35(7):591-599
    • (2006) Eur Biophys J , vol.35 , pp. 591-599
    • Paciaroni, A.1    Cornicchi, E.2    De Francesco, A.3    Marconi, M.4    Onori, G.5
  • 31
    • 29144507642 scopus 로고    scopus 로고
    • Protein dynamics on different timescales
    • Parak F, Achterhold K (2005) Protein dynamics on different timescales. J Phys Chem Solids 66:2257-2262
    • (2005) J Phys Chem Solids , vol.66 , pp. 2257-2262
    • Parak, F.1    Achterhold, K.2
  • 32
    • 84945062071 scopus 로고
    • Untersuchung des Schwingungsanteils und des Kristallgitterfehleranteils des Temperaturfaktors in Myoglobin durch Vergleich von Mö ssbauerabsorptionsmessungen mit Röntgenstrukturdaten
    • Parak F, Formanek H (1971) Untersuchung des Schwingungsanteils und des Kristallgitterfehleranteils des Temperaturfaktors in Myoglobin durch Vergleich von Mössbauerabsorptionsmessungen mit Röntgenstrukturdaten. Acta Crystallogr A 27:573-578
    • (1971) Acta Crystallogr a , vol.27 , pp. 573-578
    • Parak, F.1    Formanek, H.2
  • 33
    • 0000464216 scopus 로고
    • A consistent picture of protein dynamics
    • Parak F, Knapp EW (1984) A consistent picture of protein dynamics. PNAS USA 81:7088-7092
    • (1984) PNAS USA , vol.81 , pp. 7088-7092
    • Parak, F.1    Knapp, E.W.2
  • 34
    • 0019516596 scopus 로고
    • Dynamcis of metmyoglobin investigated by nuclear gamma-resonance absorption
    • Parak F, Frovlov EN, Mössbauer RL, Goldanskij VI (1981) Dynamcis of metmyoglobin investigated by nuclear gamma-resonance absorption. J Mol Biol 145:237-249
    • (1981) J Mol Biol , vol.145 , pp. 237-249
    • Parak, F.1    Frovlov, E.N.2    Mössbauer, R.L.3    Goldanskij, V.I.4
  • 39
    • 0036841273 scopus 로고    scopus 로고
    • Dynamic transition associated with the thermal denaturation of a small beta protein
    • Russo D, Perez J, Zanotti JM, Desmadril M, Durand D (2002) Dynamic transition associated with the thermal denaturation of a small beta protein. Biophys J 83:2792-2800
    • (2002) Biophys J , vol.83 , pp. 2792-2800
    • Russo, D.1    Perez, J.2    Zanotti, J.M.3    Desmadril, M.4    Durand, D.5
  • 40
    • 0028055167 scopus 로고
    • Calorimetric studies of the kinetic unfreezing of molecular motions in hydrated lysozyme, hemoglobin and myoglobin
    • Sartor G, Mayer E, Johari GP (1994) Calorimetric studies of the kinetic unfreezing of molecular motions in hydrated lysozyme, hemoglobin and myoglobin. Biophys J 66:249-258
    • (1994) Biophys J , vol.66 , pp. 249-258
    • Sartor, G.1    Mayer, E.2    Johari, G.P.3
  • 42
    • 0002700870 scopus 로고    scopus 로고
    • Iterative calculation of the vibrational density of states from incoherent neutron scattering data with the account of double scattering
    • Adenine Press New York. ISBN 0-940030-49-7
    • Settles M, Doster W (1997) Iterative calculation of the vibrational density of states from incoherent neutron scattering data with the account of double scattering. In: Buettner H, Cusack S, Ferrand M, Lagan P, Timmins P (eds) Biological macromolecular dynamics. Adenine Press, New York, pp 3-9. ISBN 0-940030-49-7
    • (1997) Biological Macromolecular Dynamics , pp. 3-9
    • Settles, M.1    Doster, W.2    Buettner, H.3    Cusack, S.4    Ferrand, M.5    Lagan, P.6    Timmins, P.7
  • 44
    • 0025938315 scopus 로고
    • Protein Dynamics, a comparison of simulations with inelastic neutron scattering experiments
    • Smith J (1991) Protein Dynamics, a comparison of simulations with inelastic neutron scattering experiments. Q Rev Biophys 24:227-291
    • (1991) Q Rev Biophys , vol.24 , pp. 227-291
    • Smith, J.1
  • 46
    • 0037203526 scopus 로고    scopus 로고
    • Single particle and collective dynamics of protein hydration water
    • Tarek M, Tobias D (2002) Single particle and collective dynamics of protein hydration water. Phys Rev Lett 89:13801-13804
    • (2002) Phys Rev Lett , vol.89 , pp. 13801-13804
    • Tarek, M.1    Tobias, D.2
  • 47
    • 19044399611 scopus 로고    scopus 로고
    • The role of protein-water hydrogen bonds in the dynamical transition of proteins
    • Tarek M, Tobias T (2002) The role of protein-water hydrogen bonds in the dynamical transition of proteins. Phys Rev Lett 88:381011-381013
    • (2002) Phys Rev Lett , vol.88 , pp. 381011-381013
    • Tarek, M.1    Tobias, T.2
  • 48
    • 28844498987 scopus 로고    scopus 로고
    • Neutron scattering reveals the dynamic basis of protein adaption to extreme temperature
    • Tehei M, Madern D, Franzetti B, Zaccai G (2005) Neutron scattering reveals the dynamic basis of protein adaption to extreme temperature. J Bio Chem 280:40974-40979
    • (2005) J Bio Chem , vol.280 , pp. 40974-40979
    • Tehei, M.1    Madern, D.2    Franzetti, B.3    Zaccai, G.4
  • 49
    • 33646254850 scopus 로고    scopus 로고
    • Dynamics of immobilized and native E. coli dihhydrofolate reductase by quasi-elastic neutron scattering
    • Tehei M, Smith JC, Monk C, Ollivier J, Oettl M, Kurkal V, Finney JL, Daniel RM (2006a) Dynamics of immobilized and native E. coli dihhydrofolate reductase by quasi-elastic neutron scattering. Biophys J 90:1090-1097
    • (2006) Biophys J , vol.90 , pp. 1090-1097
    • Tehei, M.1    Smith, J.C.2    Monk, C.3    Ollivier, J.4    Oettl, M.5    Kurkal, V.6    Finney, J.L.7    Daniel, R.M.8
  • 50
    • 33748559079 scopus 로고    scopus 로고
    • Fundamental and biotechnological application of neutron scattering measurements for macromolecular dynamics
    • Tehei M, Daniel R, Zaccai G (2006b) Fundamental and biotechnological application of neutron scattering measurements for macromolecular dynamics. Eur Biophys J 35:551-558
    • (2006) Eur Biophys J , vol.35 , pp. 551-558
    • Tehei, M.1    Daniel, R.2    Zaccai, G.3
  • 51
    • 0346216028 scopus 로고    scopus 로고
    • Principal components of the protein dynamical transition
    • 20
    • Tournier AL, Smith JC (2003) Principal components of the protein dynamical transition. Phys Rev Lett 91(20):208106-1-208106-4
    • (2003) Phys Rev Lett , vol.91 , pp. 2081061-12081064
    • Tournier, A.L.1    Smith, J.C.2
  • 52
    • 10444277827 scopus 로고    scopus 로고
    • Solvent caging of internal motions in myoglobin at low temperatures
    • 2
    • Tournier AL, Xu J, Smith JC (2003) Solvent caging of internal motions in myoglobin at low temperatures. Phys Chem Commun 6(2):6-8
    • (2003) Phys Chem Commun , vol.6 , pp. 6-8
    • Tournier, A.L.1    Xu, J.2    Smith, J.C.3
  • 53
    • 0033747018 scopus 로고    scopus 로고
    • Molecular dynamics of solid-state lysozyme as affected by glycerol and water, a neutron scattering study
    • Tsai AM, Neumann DA, Bell LN (2000) Molecular dynamics of solid-state lysozyme as affected by glycerol and water, a neutron scattering study. Biophys J 79:2728-2732
    • (2000) Biophys J , vol.79 , pp. 2728-2732
    • Tsai, A.M.1    Neumann, D.A.2    Bell, L.N.3
  • 54
    • 0034595671 scopus 로고    scopus 로고
    • How soft is a protein? a protein force constant measured by neutron scattering
    • Zaccai J (2000) How soft is a protein? A protein force constant measured by neutron scattering. Science 288:1604-1607
    • (2000) Science , vol.288 , pp. 1604-1607
    • Zaccai, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.