메뉴 건너뛰기




Volumn 185, Issue , 2014, Pages 25-31

Hydration dependence of myoglobin dynamics studied with elastic neutron scattering, differential scanning calorimetry and broadband dielectric spectroscopy

Author keywords

Equilibrium fluctuations; Glass transition; Hydration water liquid liquid transition; Protein dynamics; Protein hydration water relaxations

Indexed keywords

MYOGLOBIN; PROTEIN;

EID: 84888774299     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2013.11.004     Document Type: Article
Times cited : (22)

References (39)
  • 2
    • 0024976853 scopus 로고
    • Dynamical transition of myoglobin revealed by inelastic neutron scattering
    • W. Doster, S. Cusack, and W. Petry Dynamical transition of myoglobin revealed by inelastic neutron scattering Nature 337 1989 754 756
    • (1989) Nature , vol.337 , pp. 754-756
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 4
    • 58049186283 scopus 로고    scopus 로고
    • Protein fluctuations explored by inelastic neutron scattering and dielectric relaxation spectroscopy
    • G. Chen, P.W. Fenimore, H. Frauenfelder, F. Mezei, J. Swenson, and R.D. Young Protein fluctuations explored by inelastic neutron scattering and dielectric relaxation spectroscopy Philos. Mag. 88 2008 3877 3883
    • (2008) Philos. Mag. , vol.88 , pp. 3877-3883
    • Chen, G.1    Fenimore, P.W.2    Frauenfelder, H.3    Mezei, F.4    Swenson, J.5    Young, R.D.6
  • 6
    • 0034595671 scopus 로고    scopus 로고
    • How soft is a protein? A protein dynamics force constant measured by neutron scattering
    • DOI 10.1126/science.288.5471.1604
    • G. Zaccai How soft is a protein? A protein dynamics force constant measured by neutron scattering Science 288 2000 1604 1607 (Pubitemid 30387420)
    • (2000) Science , vol.288 , Issue.5471 , pp. 1604-1607
    • Zaccai, G.1
  • 8
    • 84866562225 scopus 로고    scopus 로고
    • Physical origin of anharmonic dynamics in proteins: New insights from resolution-dependent neutron scattering on homomeric polypeptides
    • G. Schirò, F. Natali, and A. Cupane Physical origin of anharmonic dynamics in proteins: new insights from resolution-dependent neutron scattering on homomeric polypeptides Phys. Rev. Lett. 109 2012 128102 128106
    • (2012) Phys. Rev. Lett. , vol.109 , pp. 128102-128106
    • Schirò, G.1    Natali, F.2    Cupane, A.3
  • 9
    • 84879821801 scopus 로고    scopus 로고
    • Anharmonic onsets in polypeptides revealed by neutron scattering: Experimental evidences and quantitative description of energy resolution dependence
    • G. Schirò Anharmonic onsets in polypeptides revealed by neutron scattering: Experimental evidences and quantitative description of energy resolution dependence Biophys. Chem. 180-181 2013 29 36
    • (2013) Biophys. Chem. , vol.180-181 , pp. 29-36
    • Schirò, G.1
  • 10
    • 84881645583 scopus 로고    scopus 로고
    • g in hydrated proteins: Trend of mean squared displacements after correcting for the methyl-group rotation contribution
    • g in hydrated proteins: Trend of mean squared displacements after correcting for the methyl-group rotation contribution J. Chem. Phys. 138 2013 235102 235115
    • (2013) J. Chem. Phys. , vol.138 , pp. 235102-235115
    • Ngai, K.L.1    Capaccioli, S.2    Paciaroni, A.3
  • 11
    • 78751568002 scopus 로고    scopus 로고
    • The two-step scenario of the protein dynamical transition
    • W. Doster The two-step scenario of the protein dynamical transition J. Non-Cryst. Solids 357 2011 622 628
    • (2011) J. Non-Cryst. Solids , vol.357 , pp. 622-628
    • Doster, W.1
  • 12
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • DOI 10.1038/35051719
    • A.M. Klibanov Improving enzymes by using them in organic solvents Nature 409 2001 241 246 (Pubitemid 32144293)
    • (2001) Nature , vol.409 , Issue.6817 , pp. 241-246
    • Klibanov, A.M.1
  • 13
    • 57049104557 scopus 로고    scopus 로고
    • Influence of hydration on protein dynamics: Combining dielectric and neutron scattering spectroscopy data
    • S. Khodadadi, S. Pawlus, and A.P. Sokolov Influence of hydration on protein dynamics: combining dielectric and neutron scattering spectroscopy data J. Phys. Chem. B 112 2008 14273 14280
    • (2008) J. Phys. Chem. B , vol.112 , pp. 14273-14280
    • Khodadadi, S.1    Pawlus, S.2    Sokolov, A.P.3
  • 14
    • 79953770674 scopus 로고    scopus 로고
    • Role of solvent for the dynamics and the glass transition of proteins
    • H. Jansson, R. Bergman, and J. Swenson Role of solvent for the dynamics and the glass transition of proteins J. Phys. Chem. B 115 2011 4099 4109
    • (2011) J. Phys. Chem. B , vol.115 , pp. 4099-4109
    • Jansson, H.1    Bergman, R.2    Swenson, J.3
  • 16
  • 17
    • 67650280467 scopus 로고    scopus 로고
    • Dielectric relaxations in confined hydrated myoglobin
    • G. Schirò, A. Cupane, E. Vitrano, and F. Bruni Dielectric relaxations in confined hydrated myoglobin J. Phys. Chem. B 113 2009 9606 9613
    • (2009) J. Phys. Chem. B , vol.113 , pp. 9606-9613
    • Schirò, G.1    Cupane, A.2    Vitrano, E.3    Bruni, F.4
  • 18
    • 84885466588 scopus 로고    scopus 로고
    • Communication: Protein dynamical transition vs. Liquid-liquid phase transition in protein hydration water
    • G. Schirò, M. Fomina, and A. Cupane Communication: Protein dynamical transition vs. liquid-liquid phase transition in protein hydration water J. Chem. Phys. 139 2013 121102
    • (2013) J. Chem. Phys. , vol.139 , pp. 121102
    • Schirò, G.1    Fomina, M.2    Cupane, A.3
  • 19
    • 41649087126 scopus 로고    scopus 로고
    • Dynamics of myoglobin in confinement: An elastic and quasi-elastic neutron scattering study
    • G. Schirò, M. Sclafani, C. Caronna, F. Natali, M. Plazanet, and A. Cupane Dynamics of myoglobin in confinement: An elastic and quasi-elastic neutron scattering study Chem. Phys. 345 2008 259 266
    • (2008) Chem. Phys. , vol.345 , pp. 259-266
    • Schirò, G.1    Sclafani, M.2    Caronna, C.3    Natali, F.4    Plazanet, M.5    Cupane, A.6
  • 20
    • 45449109193 scopus 로고    scopus 로고
    • Hydration dependent dynamics in sol-gel encapsulated myoglobin
    • G. Schirò, M. Sclafani, F. Natali, and A. Cupane Hydration dependent dynamics in sol-gel encapsulated myoglobin Eur. Biophys. J. 37 2008 543 549
    • (2008) Eur. Biophys. J. , vol.37 , pp. 543-549
    • Schirò, G.1    Sclafani, M.2    Natali, F.3    Cupane, A.4
  • 22
    • 63949086531 scopus 로고    scopus 로고
    • Insulated electrodes for eliminating conductivity in dielectric relaxation experiments
    • R. Richert Insulated electrodes for eliminating conductivity in dielectric relaxation experiments Eur. Phys. J. B 68 2009 197 200
    • (2009) Eur. Phys. J. B , vol.68 , pp. 197-200
    • Richert, R.1
  • 24
    • 77953501122 scopus 로고    scopus 로고
    • Comment on "hidden Slow Dynamics in Water"
    • R. Richert Comment on "Hidden Slow Dynamics in Water" Phys. Rev. Lett. 104 2010 249801
    • (2010) Phys. Rev. Lett. , vol.104 , pp. 249801
    • Richert, R.1
  • 25
    • 80455123688 scopus 로고    scopus 로고
    • Multiple relaxation processes versus the fragile-to-strong transition in confined water
    • F. Bruni, R. Mancinelli, and M.A. Ricci Multiple relaxation processes versus the fragile-to-strong transition in confined water Phys. Chem. Chem. Phys. 13 2011 19773 19779
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 19773-19779
    • Bruni, F.1    Mancinelli, R.2    Ricci, M.A.3
  • 27
    • 77957978218 scopus 로고    scopus 로고
    • Molecular origin and hydration dependence of protein anharmonicity: An elastic neutron scattering study
    • G. Schirò, C. Caronna, F. Natali, and A. Cupane Molecular origin and hydration dependence of protein anharmonicity: an elastic neutron scattering study Phys. Chem. Chem. Phys. 12 2010 10215 10220
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 10215-10220
    • Schirò, G.1    Caronna, C.2    Natali, F.3    Cupane, A.4
  • 28
    • 21644464858 scopus 로고    scopus 로고
    • Fast fluctuations in protein powders: The role of hydration
    • DOI 10.1016/j.cplett.2005.05.098, PII S0009261405008079
    • A. Paciaroni, S. Cinelli, E. Cornicchi, A. De Francesco, and G. Onori Fast fluctuations in protein powders: The role of hydration Chem. Phys. Lett. 410 2005 400 403 (Pubitemid 40929436)
    • (2005) Chemical Physics Letters , vol.410 , Issue.4-6 , pp. 400-403
    • Paciaroni, A.1    Cinelli, S.2    Cornicchi, E.3    De Francesco, A.4    Onori, G.5
  • 29
    • 0028845661 scopus 로고
    • Characterizing the secondary hydration shell on hydrated myoglobin, hemoglobin, and lysozyme powders by its vitrification behavior on cooling and its calorimetric glass→liquid transition and crystallization behavior on reheating
    • G. Sartor, A. Hallbrucker, and E. Mayer Characterizing the secondary hydration shell on hydrated myoglobin, hemoglobin, and lysozyme powders by its vitrification behavior on cooling and its calorimetric glass→liquid transition and crystallization behavior on reheating Biophys. J. 69 1995 2679 2694
    • (1995) Biophys. J. , vol.69 , pp. 2679-2694
    • Sartor, G.1    Hallbrucker, A.2    Mayer, E.3
  • 30
    • 0028144626 scopus 로고
    • A connected-cluster of hydration around myoglobin: Correlation between molecular dynamics simulations and experiment
    • V. Lounnas, and B.M. Pettitt A connected-cluster of hydration around myoglobin: correlation between molecular dynamics simulations and experiment Proteins 18 1994 133 147 (Pubitemid 24055076)
    • (1994) Proteins: Structure, Function and Genetics , vol.18 , Issue.2 , pp. 133-147
    • Lounnas, V.1    Pettitt, B.M.2
  • 31
    • 71649095681 scopus 로고    scopus 로고
    • The protein glass transition as measured by dielectric spectroscopy and differential scanning calorimetry
    • H. Jansson, and J. Swenson The protein glass transition as measured by dielectric spectroscopy and differential scanning calorimetry Biochim. Biophys. Acta 1804 2010 20 26
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 20-26
    • Jansson, H.1    Swenson, J.2
  • 32
    • 79956081223 scopus 로고    scopus 로고
    • Nanosecond relaxation dynamics of hydrated proteins: Water versus protein contributions
    • S. Khodadadi, J.E. Curtis, and A.P. Sokolov Nanosecond relaxation dynamics of hydrated proteins: water versus protein contributions J. Phys. Chem. B 115 2011 6222 6226
    • (2011) J. Phys. Chem. B , vol.115 , pp. 6222-6226
    • Khodadadi, S.1    Curtis, J.E.2    Sokolov, A.P.3
  • 34
    • 79959540857 scopus 로고    scopus 로고
    • Structure and dynamics of water confined in silica hydrogels: X-ray scattering and dielectric spectroscopy studies
    • M. Cammarata, M. Levantino, A. Cupane, A. Longo, A. Martorana, and F. Bruni Structure and dynamics of water confined in silica hydrogels: X-ray scattering and dielectric spectroscopy studies Eur. Phys. J. E 12 2003 S63 S66
    • (2003) Eur. Phys. J. e , vol.12
    • Cammarata, M.1    Levantino, M.2    Cupane, A.3    Longo, A.4    Martorana, A.5    Bruni, F.6
  • 35
    • 30544445880 scopus 로고    scopus 로고
    • Relation between solvent and protein dynamics as studied by dielectric spectroscopy
    • DOI 10.1021/jp052418v
    • H. Jansson, R. Bergman, and J. Swenson Relation between solvent and protein dynamics as studied by dielectric spectroscopy J. Phys. Chem. B 109 2005 24134 24141 (Pubitemid 43081463)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.50 , pp. 24134-24141
    • Jansson, H.1    Bergman, R.2    Swenson, J.3
  • 36
    • 33745408624 scopus 로고    scopus 로고
    • Relaxation processes in supercooled confined water and implications for protein dynamics
    • J. Swenson, H. Jansson, and R. Bergman Relaxation processes in supercooled confined water and implications for protein dynamics Phys. Rev. Lett. 96 2006 247802 247805
    • (2006) Phys. Rev. Lett. , vol.96 , pp. 247802-247805
    • Swenson, J.1    Jansson, H.2    Bergman, R.3
  • 37
    • 27144463970 scopus 로고    scopus 로고
    • Pressure dependence of fragile-to-strong transition and a possible second critical point in supercooled confined water
    • L. Liu, S.-H. Chen, A. Faraone, C.-W. Yen, and C.-Y. Mou Pressure dependence of fragile-to-strong transition and a possible second critical point in supercooled confined water Phys. Rev. Lett. 95 2005 117802
    • (2005) Phys. Rev. Lett. , vol.95 , pp. 117802
    • Liu, L.1    Chen, S.-H.2    Faraone, A.3    Yen, C.-W.4    Mou, C.-Y.5
  • 38
    • 79956140668 scopus 로고    scopus 로고
    • Protein thermal denaturation and matrix glass transition in different protein-trehalose-water systems
    • G. Bellavia, S. Giuffrida, G. Cottone, A. Cupane, and L. Cordone Protein thermal denaturation and matrix glass transition in different protein-trehalose-water systems J. Phys. Chem. B 115 2011 6340 6346
    • (2011) J. Phys. Chem. B , vol.115 , pp. 6340-6346
    • Bellavia, G.1    Giuffrida, S.2    Cottone, G.3    Cupane, A.4    Cordone, L.5
  • 39
    • 70349237009 scopus 로고    scopus 로고
    • Thermal denaturation of myoglobin in water-disaccharide matrixes: Relation with the glass transition of the system
    • G. Bellavia, S. Giuffrida, G. Cottone, A. Cupane, and L. Cordone Thermal denaturation of myoglobin in water-disaccharide matrixes: relation with the glass transition of the system J. Phys. Chem. B 113 2009 11543 11549
    • (2009) J. Phys. Chem. B , vol.113 , pp. 11543-11549
    • Bellavia, G.1    Giuffrida, S.2    Cottone, G.3    Cupane, A.4    Cordone, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.