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Volumn 34, Issue 2, 2014, Pages 222-235

Pressure and protein dynamism

Author keywords

biological fluctuation; dynamism of life; high pressure NMR; high energy conformers; linear and nonlinear pressure shifts

Indexed keywords

MACROMOLECULES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EID: 84901852369     PISSN: 08957959     EISSN: 14772299     Source Type: Journal    
DOI: 10.1080/08957959.2014.882917     Document Type: Article
Times cited : (12)

References (30)
  • 1
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • DOI 10.1021/bi962337c
    • Sawaya MR, Kraut J. Loop and domain movements in the mechanism of E. coli dihydrofolate reductase: crystallographic evidence. Biochemistry. 1997;36: 586-603. (Pubitemid 27057006)
    • (1997) Biochemistry , vol.36 , Issue.3 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 2
    • 0141654001 scopus 로고    scopus 로고
    • Highly fluctuating protein structures revealed by variable-pressure nuclear magnetic resonance
    • DOI 10.1021/bi034722p
    • Akasaka K. Highly fluctuating protein structures revealed by variable-pressure nuclear magnetic resonance. Biochemistry. 2003;42: 10875-10885. (Pubitemid 37174377)
    • (2003) Biochemistry , vol.42 , Issue.37 , pp. 10875-10885
    • Akasaka, K.1
  • 3
    • 0015859467 scopus 로고
    • Principles that govern the folding of proteins
    • Anfinsen C. Principles that govern the folding of proteins. Science. 1973;181: 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.1
  • 4
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland DE Jr. Application of a theory of enzyme specificity to protein synthesis. Proc Natl Acad Sci USA. 1958;44:98-104;
    • (1958) Proc Natl Acad Sci USA , vol.44 , pp. 98-104
    • Koshland Jr., D.E.1
  • 6
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux J-P. On the nature of allosteric transitions: a plausible model. J Mol Biol. 1965;12: 88-118.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 7
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H, Sligar SG, Woylnes PG. The energy landscapes and motions of proteins. Science. 1991;254: 1598-1603. (Pubitemid 21917496)
    • (1991) Science , vol.254 , Issue.5038 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 9
    • 0034912667 scopus 로고    scopus 로고
    • On-line cell high-pressure nuclear magnetic resonance technique: Application to protein studies
    • DOI 10.1016/S0076-6879(02)38218-1
    • Akasaka K, Yamada H. On-line cell high pressure nuclear magnetic resonance technique: application to protein studies. In: James TL, Dotsch V, Schmitz U, editors. Methods in enzymology 338: nuclear magnetic resonance of biological macromolecules, Part A. London: Academic Press; 2001. p. 134-158. (Pubitemid 32666577)
    • (2001) Methods in Enzymology , vol.338 , pp. 134-158
    • Akasaka, K.1    Yamada, H.2
  • 10
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • DOI 10.1016/S0022-2836(02)00241-3
    • Herrmann T, Güntert P, Wüthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol. 2002;319: 209-227. (Pubitemid 34729497)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 11
    • 0031836878 scopus 로고    scopus 로고
    • High-resolution, high-pressure NMR studies of proteins
    • Jonas J, Ballard L, Nash D. High-resolution, high-pressure NMR studies of proteins. Biophys J. 1998;75: 445-452. (Pubitemid 28311834)
    • (1998) Biophysical Journal , vol.75 , Issue.1 , pp. 445-452
    • Jonas, J.1    Ballard, L.2    Nash, D.3
  • 12
    • 0035247443 scopus 로고    scopus 로고
    • Pressure-resisting cell for high-pressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fields
    • DOI 10.1063/1.1334630
    • Yamada H, Nishikawa K, Honda M, Shimura T, Akasaka K, Tabayashi K. Pressure-resisting cell for highpressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fields. Rev Sci Inst. 2001;72: 1463-1471. (Pubitemid 33605561)
    • (2001) Review of Scientific Instruments , vol.72 , Issue.2 , pp. 1463-1471
    • Yamada, H.1    Nishikawa, K.2    Honda, M.3    Shimura, T.4    Akasaka, K.5    Tabayashi, K.6
  • 13
    • 0033136490 scopus 로고    scopus 로고
    • Preparation of encapsulated proteins dissolved in low viscosity fluids
    • DOI 10.1023/A:1008354507250
    • Ehrhardt MR, Flynn PF, Joshua Wand A. Preparation of encapsulated proteins dissolved in low viscosity fluids. J Biomol NMR. 1999;14: 75-78. (Pubitemid 29258288)
    • (1999) Journal of Biomolecular NMR , vol.14 , Issue.1 , pp. 75-78
    • Ehrhardt, M.R.1    Flynn, P.F.2    Wand, A.J.3
  • 15
    • 84866863565 scopus 로고    scopus 로고
    • Protein NMR spectroscopy: Hydrogen bonds under pressure
    • Nielsen G, Schwalbe H. Protein NMR spectroscopy: hydrogen bonds under pressure. Nat Chem. 2012;4: 693-695.
    • (2012) Nat Chem , vol.4 , pp. 693-695
    • Nielsen, G.1    Schwalbe, H.2
  • 17
    • 33646900712 scopus 로고    scopus 로고
    • Probing conformational fluctuation of proteins by pressure perturbation
    • DOI 10.1021/cr040440z
    • Akasaka K. Probing conformational fluctuation of proteins by pressure perturbation. Chem Rev. Thematic Issue 'Protein Dynamics and Folding' (Guest Editor: A. Joshua Wand) 2006;108: 1814-1835. (Pubitemid 43792782)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1814-1835
    • Akasaka, K.1
  • 18
    • 0000725483 scopus 로고
    • Thermodynamic fluctuations in protein molecules
    • Cooper A. Thermodynamic fluctuations in protein molecules. Proc Natl Acad Sci USA. 1976;73: 2740-2741.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 2740-2741
    • Cooper, A.1
  • 19
    • 0037825776 scopus 로고    scopus 로고
    • Exploring the entire conformational space of proteins by high-pressure NMR
    • Akasaka K. Exploring the entire conformational space of proteins by high-pressure NMR. Pure Appl Chem. 2003;75: 927-937.
    • (2003) Pure Appl Chem , vol.75 , pp. 927-937
    • Akasaka, K.1
  • 20
    • 78650372029 scopus 로고    scopus 로고
    • High pressureNMRstudy of proteins-seeking roots for function, evolution, disease and food applications
    • Akasaka K. High pressureNMRstudy of proteins-seeking roots for function, evolution, disease and food applications. High Pressure Res. 2010;30: 453-457.
    • (2010) High Pressure Res , vol.30 , pp. 453-457
    • Akasaka, K.1
  • 21
    • 0031554921 scopus 로고    scopus 로고
    • Pressure-induced changes in the folded structure of lysozyme
    • DOI 10.1006/jmbi.1997.1208
    • Akasaka K, Tezuka T, Yamada H. Pressure-induced changes in the folded structure of lysozyme. J Mol Biol. 1997;271: 671-678. (Pubitemid 27376045)
    • (1997) Journal of Molecular Biology , vol.271 , Issue.5 , pp. 671-678
    • Akasaka, K.1    Tezuka, T.2    Yamada, H.3
  • 22
    • 0344406172 scopus 로고    scopus 로고
    • Pressure-dependent changes in the solution structure of hen egg-white lysozyme
    • DOI 10.1016/S0022-2836(03)00209-2
    • Refaee M, Tezuka T, Akasaka K, Williamson MP. Pressure-dependent changes in the solution structure of hen egg-white lysozyme. J Mol Biol. 2003;327: 857-865. (Pubitemid 36315924)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.4 , pp. 857-865
    • Refaee, M.1    Tezuka, T.2    Akasaka, K.3    Williamson, M.P.4
  • 23
    • 79955968072 scopus 로고    scopus 로고
    • Structural characteristics of hydration sites in lysozyme
    • Soda K, Shimbo Y, Seki Y, Taiji M. Structural characteristics of hydration sites in lysozyme. Biophys Chem. 2011;156: 31-42.
    • (2011) Biophys Chem , vol.156 , pp. 31-42
    • Soda, K.1    Shimbo, Y.2    Seki, Y.3    Taiji, M.4
  • 24
    • 84884268135 scopus 로고    scopus 로고
    • Characterization of the interdomain motions in hen lysozyme using residual dipolar couplings as replica-averaged structural restraints in molecular dynamic simulations
    • Simone AD, Montalvao W, Dobson CM, Vendruscolo M. Characterization of the interdomain motions in hen lysozyme using residual dipolar couplings as replica-averaged structural restraints in molecular dynamic simulations. Biochemistry. 2013;52: 6480-6486.
    • (2013) Biochemistry , vol.52 , pp. 6480-6486
    • Simone, A.D.1    Montalvao, W.2    Dobson, C.M.3    Vendruscolo, M.4
  • 26
    • 0035979363 scopus 로고    scopus 로고
    • 15N NMR
    • DOI 10.1021/bi010312u
    • Akasaka K, Li H. Low-lying excited states of proteins revealed from nonlinear pressure shifts in 1H and 15N NMR. Biochemistry. 2001;40: 8665-8671. (Pubitemid 32709497)
    • (2001) Biochemistry , vol.40 , Issue.30 , pp. 8665-8671
    • Akasaka, K.1    Li, H.2
  • 28
    • 77649105245 scopus 로고    scopus 로고
    • Dynamic correlation between pressure-induced protein structural transition and water penetration
    • Imai T, Sugita Y. Dynamic correlation between pressure-induced protein structural transition and water penetration. J Phys Chem B. 2010;114: 2281-2286.
    • (2010) J Phys Chem B , vol.114 , pp. 2281-2286
    • Imai, T.1    Sugita, Y.2
  • 29
    • 14644424521 scopus 로고    scopus 로고
    • NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar
    • DOI 10.1016/j.jmb.2005.01.052
    • Kitahara R, Yokoyama S, Akasaka K. NMR snapshots of a fluctuating protein structure: ubiquitin at 30 bar-3 kbar. J Mol Biol. 2005;347: 277-285. (Pubitemid 40312458)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.2 , pp. 277-285
    • Kitahara, R.1    Yokoyama, S.2    Akasaka, K.3
  • 30
    • 84867743873 scopus 로고    scopus 로고
    • High-pressure macromolecular crystallography and NMR: Status, achievements and prospects
    • Fourme R, Girard E, Akasaka K. High-pressure macromolecular crystallography and NMR: status, achievements and prospects. Curr Opin Struct Biol. 2012;22: 636-642.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 636-642
    • Fourme, R.1    Girard, E.2    Akasaka, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.