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Volumn 38, Issue 2, 2009, Pages 237-244

Dynamics of apomyoglobin in the α-to-β transition and of partially unfolded aggregated protein

Author keywords

Amyloid former; Circular dichroism; Neutron; Protein dynamics

Indexed keywords


EID: 58849146097     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-008-0375-z     Document Type: Article
Times cited : (17)

References (26)
  • 1
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network
    • MA Andrade P Chacón JJ Merelo F Morán 1993 Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network Protein Eng 6 383 390
    • (1993) Protein Eng , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4
  • 2
  • 3
    • 17344393126 scopus 로고    scopus 로고
    • La diffusion quasiélastique des neutrons; Introduction et principes généraux. Diffusion Quasiélastique des Neutrons
    • M Bée 2000 La diffusion quasiélastique des neutrons; introduction et principes généraux. Diffusion Quasié lastique des Neutrons J Phys IV France 10 Pr1-1 Pr1-14
    • (2000) J Phys IV France , vol.10
    • Bée, M.1
  • 5
    • 0033580657 scopus 로고    scopus 로고
    • Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behaviour in its disease related variants
    • D Canet M Sunde AM Last A Miranker A Spencer CV Robinson CM Dobson 1999 Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behaviour in its disease related variants Biochemistry 38 6419 6427
    • (1999) Biochemistry , vol.38 , pp. 6419-6427
    • Canet, D.1    Sunde, M.2    Last, A.M.3    Miranker, A.4    Spencer, A.5    Robinson, C.V.6    Dobson, C.M.7
  • 7
    • 0035177019 scopus 로고    scopus 로고
    • Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy
    • AK Chamberlain V Receveur A Spencer C Redfield CM Dobson 2001 Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy Protein Sci 10 2525 2530
    • (2001) Protein Sci , vol.10 , pp. 2525-2530
    • Chamberlain, A.K.1    Receveur, V.2    Spencer, A.3    Redfield, C.4    Dobson, C.M.5
  • 8
    • 0024976853 scopus 로고
    • Dynamical transition of myoglobin revealed by inelastic neutron scattering
    • W Doster S Cusack W Petry 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
  • 10
    • 0027491027 scopus 로고
    • Thermal motions and function of bacteriorhodopsin in purple membranes: Effects of temperature and hydration studied by neutron scattering
    • 20
    • M Ferrand AJ Dianoux W Petry G Zaccai 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 20 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
  • 11
    • 34250363164 scopus 로고    scopus 로고
    • C-phycocyanin hydration water dynamics in the presence of trehalose: An incoherent elastic neutron scattering study at different energy resolutions
    • F Gabel MC Bellissent-Funel 2007 C-phycocyanin hydration water dynamics in the presence of trehalose: an incoherent elastic neutron scattering study at different energy resolutions Biophys J 92 4054 4063
    • (2007) Biophys J , vol.92 , pp. 4054-4063
    • Gabel, F.1    Bellissent-Funel, M.C.2
  • 13
    • 3142690417 scopus 로고    scopus 로고
    • Hierarchical map of protein unfolding and refolding at thermal equilibrium revealed by wide-angle X-ray scattering
    • M Hirai M Koizumi T Hayakawa H Takahashi S Abe H Hirai K Miura K Inoue 2004 Hierarchical map of protein unfolding and refolding at thermal equilibrium revealed by wide-angle X-ray scattering Biochemistry 43 9036 9049
    • (2004) Biochemistry , vol.43 , pp. 9036-9049
    • Hirai, M.1    Koizumi, M.2    Hayakawa, T.3    Takahashi, H.4    Abe, S.5    Hirai, H.6    Miura, K.7    Inoue, K.8
  • 15
    • 0344863187 scopus 로고    scopus 로고
    • Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: Correlation with kinetics and light-induced conformational changes
    • U Lehnert V Reat M Weik G Zaccai C Pfister 1998 Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: correlation with kinetics and light-induced conformational changes Biophys J 75 1945 1952
    • (1998) Biophys J , vol.75 , pp. 1945-1952
    • Lehnert, U.1    Reat, V.2    Weik, M.3    Zaccai, G.4    Pfister, C.5
  • 19
    • 0035997075 scopus 로고    scopus 로고
    • Effect of the environment on the protein dynamical transition: A neutron scattering study
    • A Paciaroni S Cinelli G Onori 2002 Effect of the 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
  • 20
    • 3442893560 scopus 로고    scopus 로고
    • Density of vibrational states of the light-harvesting complex II of green plants studied by inelastic neutron scattering
    • J Pieper KD Irrgang G Renger RE Lechner 2004 Density of vibrational states of the light-harvesting complex II of green plants studied by inelastic neutron scattering J Phys Chem B 108 10556 10565
    • (2004) J Phys Chem B , vol.108 , pp. 10556-10565
    • Pieper, J.1    Irrgang, K.D.2    Renger, G.3    Lechner, R.E.4
  • 22
    • 0017831702 scopus 로고
    • Physical methods for the study of myoglobin
    • TM Rothgeb FR Gurd 1978 Physical methods for the study of myoglobin Methods Enzymol 52 73 86
    • (1978) Methods Enzymol , vol.52 , pp. 73-86
    • Rothgeb, T.M.1    Gurd, F.R.2
  • 23
    • 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 E Mayer 1995 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 2679 2694
    • (1995) Biophys J , vol.69 , pp. 2679-2694
    • Sartor, G.1    Hallbrucker, A.2    Mayer, E.3
  • 24
    • 0035165190 scopus 로고    scopus 로고
    • The stability and folding process of amyloidogenic mutant human lysozymes
    • 1
    • K Takano J Funahashi K Yutani 2001 The stability and folding process of amyloidogenic mutant human lysozymes Eur J Biochem 268 1 155 159
    • (2001) Eur J Biochem , vol.268 , pp. 155-159
    • Takano, K.1    Funahashi, J.2    Yutani, K.3
  • 26
    • 0034595671 scopus 로고    scopus 로고
    • How soft is a protein? a protein dynamics force constant measured by neutron scattering
    • G Zaccai 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.