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Volumn 8, Issue 10, 2012, Pages 3445-3451

On the use of experimental observations to bias simulated ensembles

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EID: 84867371299     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/ct300112v     Document Type: Article
Times cited : (207)

References (21)
  • 2
    • 0027293559 scopus 로고
    • Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMR-spectroscopy
    • Brunger, A. T.; Nilges, M. Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMR-spectroscopy Q. Rev. Biophys. 1993, 26 (1) 49-125
    • (1993) Q. Rev. Biophys. , vol.26 , Issue.1 , pp. 49-125
    • Brunger, A.T.1    Nilges, M.2
  • 3
    • 0022419169 scopus 로고
    • A protein structure from nuclear magnetic resonance data. lac repressor headpiece
    • Kaptein, R.; Zuiderweg, E. R.; Scheek, R. M.; Boelens, R.; van Gunsteren, W. F. A protein structure from nuclear magnetic resonance data. lac repressor headpiece J. Mol. Biol. 1985, 182 (1) 179-182
    • (1985) J. Mol. Biol. , vol.182 , Issue.1 , pp. 179-182
    • Kaptein, R.1    Zuiderweg, E.R.2    Scheek, R.M.3    Boelens, R.4    Van Gunsteren, W.F.5
  • 4
    • 0000114713 scopus 로고
    • Conformational Dynamics Detected by Nuclear Magnetic Resonance NOE Values and J Coupling Constants
    • Kessler, H.; Griesinger, C.; Lautz, J.; Mueller, A.; van Gunsteren, W. F.; Berendsen, H. J. C. Conformational Dynamics Detected by Nuclear Magnetic Resonance NOE Values and J Coupling Constants J. Am. Chem. Soc. 1988, 110 (11) 3393-3396
    • (1988) J. Am. Chem. Soc. , vol.110 , Issue.11 , pp. 3393-3396
    • Kessler, H.1    Griesinger, C.2    Lautz, J.3    Mueller, A.4    Van Gunsteren, W.F.5    Berendsen, H.J.C.6
  • 5
    • 0027352894 scopus 로고
    • Structure refinement using time-averaged J-coupling constant restraints
    • Torda, A. E.; Brunne, R. M.; Huber, T.; Kessler, H.; van Gunsteren, W. F. Structure refinement using time-averaged J-coupling constant restraints J Biomol. NMR 1993, 3 (1) 55-66
    • (1993) J Biomol. NMR , vol.3 , Issue.1 , pp. 55-66
    • Torda, A.E.1    Brunne, R.M.2    Huber, T.3    Kessler, H.4    Van Gunsteren, W.F.5
  • 6
    • 0025367860 scopus 로고
    • Time-averaged nuclear Overhauser effect distance restraints applied to Tendamistat
    • Torda, A. E.; Scheek, R. M.; van Gunsteren, W. F. Time-averaged nuclear Overhauser effect distance restraints applied to Tendamistat J. Mol. Biol. 1990, 214 (1) 223-235
    • (1990) J. Mol. Biol. , vol.214 , Issue.1 , pp. 223-235
    • Torda, A.E.1    Scheek, R.M.2    Van Gunsteren, W.F.3
  • 8
    • 3042846748 scopus 로고    scopus 로고
    • Determination of protein structures consistent with NMR order parameters
    • Best, R. B.; Vendruscolo, M. Determination of protein structures consistent with NMR order parameters J. Am. Chem. Soc. 2004, 126 (26) 8090-8091
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.26 , pp. 8090-8091
    • Best, R.B.1    Vendruscolo, M.2
  • 9
    • 0035028578 scopus 로고    scopus 로고
    • Assessing the effect of conformational averaging on the measured values of observables
    • Burgi, R.; Pitera, J.; van Gunsteren, W. F. Assessing the effect of conformational averaging on the measured values of observables J. Biomol. NMR 2001, 19 (4) 305-320
    • (2001) J. Biomol. NMR , vol.19 , Issue.4 , pp. 305-320
    • Burgi, R.1    Pitera, J.2    Van Gunsteren, W.F.3
  • 10
    • 0033394128 scopus 로고    scopus 로고
    • Maximum entropy approach to the determination of solution conformation of flexible polypeptides by global conformational analysis and NMR spectroscopy - Application to DNS1-c-[D-A2,bu2,Trp4,Leu5]enkephalin and DNS1-c-[D-A2bu2,Trp4,D- Leu5]enkephalin
    • Groth, M.; Malicka, J.; Czaplewski, C.; Oldziej, S.; Lankiewicz, L.; Wiczk, W.; Liwo, A. Maximum entropy approach to the determination of solution conformation of flexible polypeptides by global conformational analysis and NMR spectroscopy - application to DNS1-c-[D-A2,bu2,Trp4,Leu5]enkephalin and DNS1-c-[D-A2bu2,Trp4,D-Leu5]enkephalin J. Biomol. NMR 1999, 15 (4) 315-330
    • (1999) J. Biomol. NMR , vol.15 , Issue.4 , pp. 315-330
    • Groth, M.1    Malicka, J.2    Czaplewski, C.3    Oldziej, S.4    Lankiewicz, L.5    Wiczk, W.6    Liwo, A.7
  • 11
    • 33846783019 scopus 로고    scopus 로고
    • Structure and dynamics of the homologous series of alanine peptides: A joint molecular dynamics/NMR study
    • Graf, J.; Nguyen, P. H.; Stock, G.; Schwalbe, H. Structure and dynamics of the homologous series of alanine peptides: a joint molecular dynamics/NMR study J. Am. Chem. Soc. 2007, 129 (5) 1179-1189
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.5 , pp. 1179-1189
    • Graf, J.1    Nguyen, P.H.2    Stock, G.3    Schwalbe, H.4
  • 12
    • 78650948314 scopus 로고    scopus 로고
    • SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions
    • Rozycki, B.; Kim, Y. C.; Hummer, G. SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions Structure 2011, 19 (1) 109-116
    • (2011) Structure , vol.19 , Issue.1 , pp. 109-116
    • Rozycki, B.1    Kim, Y.C.2    Hummer, G.3
  • 13
    • 0036424048 scopus 로고    scopus 로고
    • Transition path sampling: Throwing ropes over rough mountain passes, in the dark
    • Bolhuis, P. G.; Chandler, D.; Dellago, C.; Geissler, P. L. Transition path sampling: throwing ropes over rough mountain passes, in the dark Annu. Rev. Phys. Chem. 2002, 53, 291-318
    • (2002) Annu. Rev. Phys. Chem. , vol.53 , pp. 291-318
    • Bolhuis, P.G.1    Chandler, D.2    Dellago, C.3    Geissler, P.L.4
  • 14
    • 22144489530 scopus 로고    scopus 로고
    • Inferential structure determination
    • Rieping, W.; Habeck, M.; Nilges, M. Inferential structure determination Science 2005, 309 (5732) 303-306
    • (2005) Science , vol.309 , Issue.5732 , pp. 303-306
    • Rieping, W.1    Habeck, M.2    Nilges, M.3
  • 15
    • 11944266539 scopus 로고
    • Information Theory and Statistical Mechanics
    • Jaynes, E. T. Information Theory and Statistical Mechanics Phys. Rev. 1957, 106 (4) 620-630
    • (1957) Phys. Rev. , vol.106 , Issue.4 , pp. 620-630
    • Jaynes, E.T.1
  • 16
    • 7244247445 scopus 로고
    • Maximum entropy in the problem of moments
    • Mead, L. R.; Papanicolaou, N. Maximum entropy in the problem of moments J. Math. Phys. 1984, 25 (8) 2404-2417
    • (1984) J. Math. Phys. , vol.25 , Issue.8 , pp. 2404-2417
    • Mead, L.R.1    Papanicolaou, N.2
  • 17
    • 52949088587 scopus 로고    scopus 로고
    • Statistically optimal analysis of samples from multiple equilibrium states
    • Shirts, M. R.; Chodera, J. D. Statistically optimal analysis of samples from multiple equilibrium states J. Chem. Phys. 2008, 129 (12) 124105
    • (2008) J. Chem. Phys. , vol.129 , Issue.12 , pp. 124105
    • Shirts, M.R.1    Chodera, J.D.2
  • 18
    • 0001628105 scopus 로고
    • Determination of force field parameters for molecular simulation by molecular simulation: An application of the weak-coupling method
    • Njo, S. L.; van Gunsteren, W. F.; Mueller-Plathe, F. Determination of force field parameters for molecular simulation by molecular simulation: An application of the weak-coupling method J. Chem. Phys. 1995, 102 (15) 6199-6207
    • (1995) J. Chem. Phys. , vol.102 , Issue.15 , pp. 6199-6207
    • Njo, S.L.1    Van Gunsteren, W.F.2    Mueller-Plathe, F.3
  • 19
    • 0025778738 scopus 로고
    • Are time-averaged restraints necessary for nuclear magnetic resonance refinement? A model study for DNA
    • Pearlman, D. A.; Kollman, P. A. Are time-averaged restraints necessary for nuclear magnetic resonance refinement? A model study for DNA J. Mol. Biol. 1991, 220 (2) 457-479
    • (1991) J. Mol. Biol. , vol.220 , Issue.2 , pp. 457-479
    • Pearlman, D.A.1    Kollman, P.A.2
  • 20
    • 0029365350 scopus 로고
    • Structure refinement with molecular dynamics and a Boltzmann-weighted ensemble
    • Fennen, J.; Torda, A. E.; van Gunsteren, W. F. Structure refinement with molecular dynamics and a Boltzmann-weighted ensemble J. Biomol. NMR 1995, 6 (2) 163-170
    • (1995) J. Biomol. NMR , vol.6 , Issue.2 , pp. 163-170
    • Fennen, J.1    Torda, A.E.2    Van Gunsteren, W.F.3
  • 21
    • 33846532929 scopus 로고    scopus 로고
    • The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native state ensembles of proteins
    • Richter, B.; Gsponer, J.; Varnai, P.; Salvatella, X.; Vendruscolo, M. The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native state ensembles of proteins J. Biomol. NMR 2007, 37 (2) 117-135
    • (2007) J. Biomol. NMR , vol.37 , Issue.2 , pp. 117-135
    • Richter, B.1    Gsponer, J.2    Varnai, P.3    Salvatella, X.4    Vendruscolo, M.5


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