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Volumn 6, Issue MAY, 2015, Pages

Information flow and protein dynamics: The interplay between nuclear magnetic resonance spectroscopy and molecular dynamics simulations

Author keywords

Aggregation; Allosterism; Binding; Dynamics; Folding intermediates

Indexed keywords


EID: 84934878563     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2015.00306     Document Type: Review
Times cited : (14)

References (96)
  • 1
    • 84883488802 scopus 로고    scopus 로고
    • Active site conformational dynamics are coupled to catalysis in the mRNA decapping enzyme Dcp2
    • Aglietti, R. A., Floor, S. N., McClendon, C. L., Jacobson, M. P., and Gross, J. D. (2013). Active site conformational dynamics are coupled to catalysis in the mRNA decapping enzyme Dcp2. Structure 21, 1571-1580. doi: 10. 1016/j. str. 2013. 06. 021.
    • (2013) Structure , vol.21 , pp. 1571-1580
    • Aglietti, R.A.1    Floor, S.N.2    McClendon, C.L.3    Jacobson, M.P.4    Gross, J.D.5
  • 2
    • 84873151853 scopus 로고    scopus 로고
    • Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data
    • Allison, J. R. (2012). Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data. Biophys. Rev. 4, 189-203. doi: 10. 1007/s12551-012-0087-6.
    • (2012) Biophys. Rev , vol.4 , pp. 189-203
    • Allison, J.R.1
  • 3
    • 84867365389 scopus 로고    scopus 로고
    • Probing the structure and dynamics of proteins by combining molecular dynamics simulations and experimental NMR data
    • Allison, J. R., Hertig, S., Missimer, J. H., Smith, L. J., Steinmetz, M. O., and Dolenc, J. (2012). Probing the structure and dynamics of proteins by combining molecular dynamics simulations and experimental NMR data. J. Chem. Theory Comput. 8, 3430-3444. doi: 10. 1021/ct300393b.
    • (2012) J. Chem. Theory Comput , vol.8 , pp. 3430-3444
    • Allison, J.R.1    Hertig, S.2    Missimer, J.H.3    Smith, L.J.4    Steinmetz, M.O.5    Dolenc, J.6
  • 4
    • 84921492193 scopus 로고    scopus 로고
    • Motions and entropies in proteins as seen in NMR relaxation experiments and molecular dynamics simulations
    • Allnér, O., Foloppe, N., and Nilsson, L. (2015). Motions and entropies in proteins as seen in NMR relaxation experiments and molecular dynamics simulations. J. Phys. Chem. B 119, 1114-1128. doi: 10. 1021/jp506609g.
    • (2015) J. Phys. Chem. B , vol.119 , pp. 1114-1128
    • Allnér, O.1    Foloppe, N.2    Nilsson, L.3
  • 5
    • 84898545475 scopus 로고    scopus 로고
    • Insights into the binding of intrinsically disordered proteins from molecular dynamics simulation
    • Baker, C. M., and Best, R. B. (2014). Insights into the binding of intrinsically disordered proteins from molecular dynamics simulation. Wiley Interdiscip. Rev. Comput. Mol. Sci. 4, 182-198. doi: 10. 1002/wcms. 1167.
    • (2014) Wiley Interdiscip. Rev. Comput. Mol. Sci , vol.4 , pp. 182-198
    • Baker, C.M.1    Best, R.B.2
  • 6
    • 84883226851 scopus 로고    scopus 로고
    • Use of a small peptide fragment as an inhibitor of insulin fibrillation process: A study by high and low resolution spectroscopy
    • Banerjee, V., Kar, R. K., Datta, A., Parthasarathi, K., Chatterjee, S., Das, K. P., et al. (2013). Use of a small peptide fragment as an inhibitor of insulin fibrillation process: a study by high and low resolution spectroscopy. PLoS ONE 8: e72318. doi: 10. 1371/journal. pone. 0072318.
    • (2013) PLoS ONE , vol.8
    • Banerjee, V.1    Kar, R.K.2    Datta, A.3    Parthasarathi, K.4    Chatterjee, S.5    Das, K.P.6
  • 7
    • 84905035389 scopus 로고    scopus 로고
    • Computing protein dynamics from protein structure with elastic network models
    • Bastolla, U. (2014). Computing protein dynamics from protein structure with elastic network models. Wiley Interdiscip. Rev. Comput. Mol. Sci. 4, 488-503. doi: 10. 1002/wcms. 1186.
    • (2014) Wiley Interdiscip. Rev. Comput. Mol. Sci , vol.4 , pp. 488-503
    • Bastolla, U.1
  • 8
    • 84858978818 scopus 로고    scopus 로고
    • Protein misfolded oligomers: Experimental approaches, mechanism of formation, and structure-toxicity relationships
    • Bemporad, F., and Chiti, F. (2012). Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships. Chem. Biol. 19, 315-327. doi: 10. 1016/j. chembiol. 2012. 02. 003.
    • (2012) Chem. Biol , vol.19 , pp. 315-327
    • Bemporad, F.1    Chiti, F.2
  • 9
    • 84861872576 scopus 로고    scopus 로고
    • Characterizing intermolecular interactions that initiate native-like protein aggregation
    • Bemporad, F., De Simone, A., Chiti, F., and Dobson, C. M. (2012). Characterizing intermolecular interactions that initiate native-like protein aggregation. Biophys. J. 102, 2595-2604. doi: 10. 1016/j. bpj. 2012. 03. 057.
    • (2012) Biophys. J , vol.102 , pp. 2595-2604
    • Bemporad, F.1    De Simone, A.2    Chiti, F.3    Dobson, C.M.4
  • 10
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein, F. C., Koetzle, T. F., Williams, G. J., Meyer, E. F., Brice, M. D., Rodgers, J. R., et al. (1977). The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542. doi: 10. 1016/S0022-2836(77)80200-3.
    • (1977) J. Mol. Biol , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Koetzle, T.F.2    Williams, G.J.3    Meyer, E.F.4    Brice, M.D.5    Rodgers, J.R.6
  • 11
    • 79951931431 scopus 로고    scopus 로고
    • Macromolecular NMR spectroscopy for the non-spectroscopist: Beyond macromolecular solution structure determination
    • Bieri, M., Kwan, A. H., Mobli, M., King, G. F., Mackay, J. P., and Gooley, P. R. (2011). Macromolecular NMR spectroscopy for the non-spectroscopist: beyond macromolecular solution structure determination. FEBS J. 278, 704-715. doi: 10. 1111/j. 1742-4658. 2011. 08005. x.
    • (2011) FEBS J , vol.278 , pp. 704-715
    • Bieri, M.1    Kwan, A.H.2    Mobli, M.3    King, G.F.4    Mackay, J.P.5    Gooley, P.R.6
  • 12
    • 84856414506 scopus 로고    scopus 로고
    • Residual structure in unfolded proteins
    • Bowler, B. E. (2012). Residual structure in unfolded proteins. Curr. Opin. Struct. Biol. 22, 4-13. doi: 10. 1016/j. sbi. 2011. 09. 002.
    • (2012) Curr. Opin. Struct. Biol , vol.22 , pp. 4-13
    • Bowler, B.E.1
  • 14
    • 84857787795 scopus 로고    scopus 로고
    • Insights into internal dynamics of 6-phosphogluconolactonase from Trypanosoma brucei studied by nuclear magnetic resonance and molecular dynamics
    • Calligari, P. A., Salgado, G. F., Pelupessy, P., Lopes, P., Ouazzani, J., Bodenhausen, G., et al. (2012). Insights into internal dynamics of 6-phosphogluconolactonase from Trypanosoma brucei studied by nuclear magnetic resonance and molecular dynamics. Proteins 80, 1196-1210. doi: 10. 1002/prot. 24019.
    • (2012) Proteins , vol.80 , pp. 1196-1210
    • Calligari, P.A.1    Salgado, G.F.2    Pelupessy, P.3    Lopes, P.4    Ouazzani, J.5    Bodenhausen, G.6
  • 15
    • 84878537787 scopus 로고    scopus 로고
    • Chemical shifts in biomolecules
    • Case, D. A. (2013). Chemical shifts in biomolecules. Curr. Opin. Struct. Biol. 23, 172-176. doi: 10. 1016/j. sbi. 2013. 01. 007.
    • (2013) Curr. Opin. Struct. Biol , vol.23 , pp. 172-176
    • Case, D.A.1
  • 16
    • 84888333782 scopus 로고    scopus 로고
    • 50 years of allosteric interactions: The twists and turns of the models
    • Changeux, J.-P. (2013). 50 years of allosteric interactions: the twists and turns of the models. Nat. Rev. Mol. Cell Biol. 14, 819-829. doi: 10. 1038/nrm3695.
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 819-829
    • Changeux, J.-P.1
  • 17
    • 84900548447 scopus 로고    scopus 로고
    • Markov state models of biomolecular conformational dynamics
    • Chodera, J. D., and Noé, F. (2014). Markov state models of biomolecular conformational dynamics. Curr. Opin. Struct. Biol. 25, 135-144. doi: 10. 1016/j. sbi. 2014. 04. 002.
    • (2014) Curr. Opin. Struct. Biol , vol.25 , pp. 135-144
    • Chodera, J.D.1    Noé, F.2
  • 18
    • 80051985182 scopus 로고    scopus 로고
    • The social network (of protein conformations)
    • Chodera, J. D., and Pande, V. S. (2011). The social network (of protein conformations). Proc. Natl. Acad. Sci. U. S. A. 108, 12969-12970. doi: 10. 1073/pnas. 1109571108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 12969-12970
    • Chodera, J.D.1    Pande, V.S.2
  • 19
    • 84927979910 scopus 로고    scopus 로고
    • Making biomolecular simulations accessible in the post-nobel prize era
    • Cui, Q., and Nussinov, R. (2014). Making biomolecular simulations accessible in the post-nobel prize era. PLoS Comput. Biol. 10: e1003786. doi: 10. 1371/journal. pcbi. 1003786.
    • (2014) PLoS Comput. Biol , vol.10
    • Cui, Q.1    Nussinov, R.2
  • 20
    • 84883366531 scopus 로고    scopus 로고
    • Effective harmonic potentials: Insights into the internal cooperativity and sequence-specificity of protein dynamics
    • Dehouck, Y., and Mikhailov, A. S. (2013). Effective harmonic potentials: insights into the internal cooperativity and sequence-specificity of protein dynamics. PLoS Comput. Biol. 9: e1003209. doi: 10. 1371/journal. pcbi. 1003209.
    • (2013) PLoS Comput. Biol , vol.9
    • Dehouck, Y.1    Mikhailov, A.S.2
  • 21
    • 84884825977 scopus 로고    scopus 로고
    • A molecular dynamics simulation-based interpretation of nuclear magnetic resonance multidimensional heteronuclear spectra of α-synuclein·dopamine adducts
    • Dibenedetto, D., Rossetti, G., Caliandro, R., and Carloni, P. (2013). A molecular dynamics simulation-based interpretation of nuclear magnetic resonance multidimensional heteronuclear spectra of α-synuclein·dopamine adducts. Biochemistry 52, 6672-6683. doi: 10. 1021/bi400367r.
    • (2013) Biochemistry , vol.52 , pp. 6672-6683
    • Dibenedetto, D.1    Rossetti, G.2    Caliandro, R.3    Carloni, P.4
  • 22
    • 84861367246 scopus 로고    scopus 로고
    • Biomolecular simulation: A computational microscope for molecular biology
    • Dror, R. O., Dirks, R. M., Grossman, J. P., Xu, H., and Shaw, D. E. (2012). Biomolecular simulation: a computational microscope for molecular biology. Annu. Rev. Biophys. 41, 429-452. doi: 10. 1146/annurev-biophys-042910-155245.
    • (2012) Annu. Rev. Biophys , vol.41 , pp. 429-452
    • Dror, R.O.1    Dirks, R.M.2    Grossman, J.P.3    Xu, H.4    Shaw, D.E.5
  • 23
    • 79953100071 scopus 로고    scopus 로고
    • Simulations of allosteric transitions
    • Elber, R. (2011). Simulations of allosteric transitions. Curr. Opin. Struct. Biol. 21, 167-172. doi: 10. 1016/j. sbi. 2011. 01. 012.
    • (2011) Curr. Opin. Struct. Biol , vol.21 , pp. 167-172
    • Elber, R.1
  • 24
    • 84859909909 scopus 로고    scopus 로고
    • Synergistic use of NMR and MD simulations to study the structural heterogeneity of proteins
    • Esteban-Martin, S., Bryn Fenwick, R., and Salvatella, X. (2012). Synergistic use of NMR and MD simulations to study the structural heterogeneity of proteins. Wiley Interdiscip. Rev. Comput. Mol. Sci. 2, 466-478. doi: 10. 1002/wcms. 1093.
    • (2012) Wiley Interdiscip. Rev. Comput. Mol. Sci , vol.2 , pp. 466-478
    • Esteban-Martin, S.1    Bryn Fenwick, R.2    Salvatella, X.3
  • 25
    • 84883629745 scopus 로고    scopus 로고
    • Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein
    • Esteban-Martin, S., Silvestre-Ryan, J., Bertoncini, C. W., and Salvatella, X. (2013). Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein. Biophys. J. 105, 1192-1198. doi: 10. 1016/j. bpj. 2013. 07. 044.
    • (2013) Biophys. J , vol.105 , pp. 1192-1198
    • Esteban-Martin, S.1    Silvestre-Ryan, J.2    Bertoncini, C.W.3    Salvatella, X.4
  • 26
    • 84896484176 scopus 로고    scopus 로고
    • Computational approaches to mapping allosteric pathways
    • Feher, V. A., Durrant, J. D., Van Wart, A. T., and Amaro, R. E. (2014). Computational approaches to mapping allosteric pathways. Curr. Opin. Struct. Biol. 25, 98-103. doi: 10. 1016/j. sbi. 2014. 02. 004.
    • (2014) Curr. Opin. Struct. Biol , vol.25 , pp. 98-103
    • Feher, V.A.1    Durrant, J.D.2    Van Wart, A.T.3    Amaro, R.E.4
  • 27
    • 84858135911 scopus 로고    scopus 로고
    • Synergistic applications of MD and NMR for the study of biological systems
    • Fisette, O., Lagüe, P., Gagné, S., and Morin, S. (2012). Synergistic applications of MD and NMR for the study of biological systems. J. Biomed. Biotechnol. 2012, 254208. doi: 10. 1155/2012/254208.
    • (2012) J. Biomed. Biotechnol , vol.2012
    • Fisette, O.1    Lagüe, P.2    Gagné, S.3    Morin, S.4
  • 28
    • 84902500178 scopus 로고    scopus 로고
    • Controlling entropy to tune the functions of intrinsically disordered regions
    • Flock, T., Weatheritt, R. J., Latysheva, N. S., and Babu, M. M. (2014). Controlling entropy to tune the functions of intrinsically disordered regions. Curr. Opin. Struct. Biol. 26, 62-72. doi: 10. 1016/j. sbi. 2014. 05. 007.
    • (2014) Curr. Opin. Struct. Biol , vol.26 , pp. 62-72
    • Flock, T.1    Weatheritt, R.J.2    Latysheva, N.S.3    Babu, M.M.4
  • 29
    • 33846285730 scopus 로고    scopus 로고
    • Solution NMR of large molecules and assemblies
    • Foster, M. P., McElroy, C. A., and Amero, C. (2007). Solution NMR of large molecules and assemblies. Biochemistry 46, 331-340. doi: 10. 1021/bi0621314.
    • (2007) Biochemistry , vol.46 , pp. 331-340
    • Foster, M.P.1    McElroy, C.A.2    Amero, C.3
  • 30
    • 84898864167 scopus 로고    scopus 로고
    • The importance of intrinsic order in a disordered protein ligand
    • Goto, N. K. (2014). The importance of intrinsic order in a disordered protein ligand. Biophys. J. 106, 1557-1558. doi: 10. 1016/j. bpj. 2014. 03. 005.
    • (2014) Biophys. J , vol.106 , pp. 1557-1558
    • Goto, N.K.1
  • 31
    • 84876837158 scopus 로고    scopus 로고
    • Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics
    • Granata, D., Camilloni, C., Vendruscolo, M., and Laio, A. (2013). Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics. Proc. Natl. Acad. Sci. U. S. A. 110, 6817-6822. doi: 10. 1073/pnas. 1218350110.
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110 , pp. 6817-6822
    • Granata, D.1    Camilloni, C.2    Vendruscolo, M.3    Laio, A.4
  • 32
    • 84934878997 scopus 로고    scopus 로고
    • Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen
    • Grutsch, S., Fuchs, J. E., Freier, R., Kofler, S., Bibi, M., Asam, C., et al. (2014). Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen. Biophys. J. 107, 2963-2972. doi: 10. 1016/j. bpj. 2014. 10. 062.
    • (2014) Biophys. J , vol.107 , pp. 2963-2972
    • Grutsch, S.1    Fuchs, J.E.2    Freier, R.3    Kofler, S.4    Bibi, M.5    Asam, C.6
  • 33
    • 84874867093 scopus 로고    scopus 로고
    • Mapping the population of protein conformational energy sub-states from NMR dipolar couplings
    • Guerry, P., Salmon, L., Mollica, L., Ortega Roldan, J.-L., Markwick, P. R. L., van Nuland, N. A. J., et al. (2013). Mapping the population of protein conformational energy sub-states from NMR dipolar couplings. Angew. Chem. 52, 3181-3185. doi: 10. 1002/anie. 201209669.
    • (2013) Angew. Chem , vol.52 , pp. 3181-3185
    • Guerry, P.1    Salmon, L.2    Mollica, L.3    Ortega Roldan, J.-L.4    Markwick, P.R.L.5    van Nuland, N.A.J.6
  • 34
    • 84874843784 scopus 로고    scopus 로고
    • Reduced native state stability in crowded cellular environment due to protein-protein interactions
    • Harada, R., Tochio, N., Kigawa, T., Sugita, Y., and Feig, M. (2013). Reduced native state stability in crowded cellular environment due to protein-protein interactions. J. Am. Chem. Soc. 135, 3696-3701. doi: 10. 1021/ja3126992.
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 3696-3701
    • Harada, R.1    Tochio, N.2    Kigawa, T.3    Sugita, Y.4    Feig, M.5
  • 35
    • 84890732889 scopus 로고    scopus 로고
    • Structure determination of protein-protein complexes with long-range anisotropic paramagnetic NMR restraints
    • Hass, M. A., and Ubbink, M. (2014). Structure determination of protein-protein complexes with long-range anisotropic paramagnetic NMR restraints. Curr. Opin. Struct. Biol. 24, 45-53. doi: 10. 1016/j. sbi. 2013. 11. 010.
    • (2014) Curr. Opin. Struct. Biol , vol.24 , pp. 45-53
    • Hass, M.A.1    Ubbink, M.2
  • 36
    • 84884549365 scopus 로고    scopus 로고
    • Unique structure and dynamics of the EphA5 ligand binding domain mediate its binding specificity as revealed by X-ray crystallography, NMR and MD simulations
    • Huan, X., Shi, J., Lim, L., Mitra, S., Zhu, W., Qin, H., et al. (2013). Unique structure and dynamics of the EphA5 ligand binding domain mediate its binding specificity as revealed by X-ray crystallography, NMR and MD simulations. PLoS ONE 8: e74040. doi: 10. 1371/journal. pone. 0074040.
    • (2013) PLoS ONE , vol.8
    • Huan, X.1    Shi, J.2    Lim, L.3    Mitra, S.4    Zhu, W.5    Qin, H.6
  • 38
    • 84887305278 scopus 로고    scopus 로고
    • Ligand clouds around protein clouds: A scenario of ligand binding with intrinsically disordered proteins
    • Jin, F., Yu, C., Lai, L., and Liu, Z. (2013). Ligand clouds around protein clouds: a scenario of ligand binding with intrinsically disordered proteins. PLoS Comput. Biol. 9: e1003249. doi: 10. 1371/journal. pcbi. 1003249.
    • (2013) PLoS Comput. Biol , vol.9
    • Jin, F.1    Yu, C.2    Lai, L.3    Liu, Z.4
  • 39
    • 84894165236 scopus 로고    scopus 로고
    • A conformational ensemble derived using NMR methyl chemical shifts reveals a mechanical clamping transition that gates the binding of the HU protein to DNA
    • Kannan, A., Camilloni, C., Sahakyan, A. B., Cavalli, A., and Vendruscolo, M. (2014). A conformational ensemble derived using NMR methyl chemical shifts reveals a mechanical clamping transition that gates the binding of the HU protein to DNA. J. Am. Chem. Soc. 136, 2204-2207. doi: 10. 1021/ja4105396.
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 2204-2207
    • Kannan, A.1    Camilloni, C.2    Sahakyan, A.B.3    Cavalli, A.4    Vendruscolo, M.5
  • 40
    • 84888835711 scopus 로고    scopus 로고
    • Molecular origins of binding affinity: Seeking the Archimedean point
    • Kastritis, P. L., and Bonvin, A. M. J. J. (2013). Molecular origins of binding affinity: seeking the Archimedean point. Curr. Opin. Struct. Biol. 23, 868-877. doi: 10. 1016/j. sbi. 2013. 07. 001.
    • (2013) Curr. Opin. Struct. Biol , vol.23 , pp. 868-877
    • Kastritis, P.L.1    Bonvin, A.M.J.J.2
  • 41
    • 79958837339 scopus 로고    scopus 로고
    • An introduction to NMR-based approaches for measuring protein dynamics
    • Kleckner, I. R., and Foster, M. P. (2011). An introduction to NMR-based approaches for measuring protein dynamics. Biochim. Biophys. Acta 1814, 942-968. doi: 10. 1016/j. bbapap. 2010. 10. 012.
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 942-968
    • Kleckner, I.R.1    Foster, M.P.2
  • 42
    • 84900836393 scopus 로고    scopus 로고
    • Design and application of implicit solvent models in biomolecular simulations
    • Kleinjung, J., and Fraternali, F. (2014). Design and application of implicit solvent models in biomolecular simulations. Curr. Opin. Struct. Biol. 25, 126-134. doi: 10. 1016/j. sbi. 2014. 04. 003.
    • (2014) Curr. Opin. Struct. Biol , vol.25 , pp. 126-134
    • Kleinjung, J.1    Fraternali, F.2
  • 43
    • 84901355639 scopus 로고    scopus 로고
    • The amyloid state and its association with protein misfolding diseases
    • Knowles, T. P. J., Vendruscolo, M., and Dobson, C. M. (2014). The amyloid state and its association with protein misfolding diseases. Nat. Rev. Mol. Cell Biol. 15, 384-396. doi: 10. 1038/nrm3810.
    • (2014) Nat. Rev. Mol. Cell Biol , vol.15 , pp. 384-396
    • Knowles, T.P.J.1    Vendruscolo, M.2    Dobson, C.M.3
  • 44
    • 84898851755 scopus 로고    scopus 로고
    • Conformational recognition of an intrinsically disordered protein
    • Krieger, J. M., Fusco, G., Lewitzky, M., Simister, P. C., Marchant, J., Camilloni, C., et al. (2014). Conformational recognition of an intrinsically disordered protein. Biophys. J. 106, 1771-1779. doi: 10. 1016/j. bpj. 2014. 03. 004.
    • (2014) Biophys. J , vol.106 , pp. 1771-1779
    • Krieger, J.M.1    Fusco, G.2    Lewitzky, M.3    Simister, P.C.4    Marchant, J.5    Camilloni, C.6
  • 45
    • 84897114194 scopus 로고    scopus 로고
    • Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts
    • Kukic, P., Camilloni, C., Cavalli, A., and Vendruscolo, M. (2014). Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts. J. Mol. Biol. 426, 1826-1838. doi: 10. 1016/j. jmb. 2014. 02. 002.
    • (2014) J. Mol. Biol , vol.426 , pp. 1826-1838
    • Kukic, P.1    Camilloni, C.2    Cavalli, A.3    Vendruscolo, M.4
  • 46
    • 84873526912 scopus 로고    scopus 로고
    • To milliseconds and beyond: Challenges in the simulation of protein folding
    • Lane, T. J., Shukla, D., Beauchamp, K. A., and Pande, V. S. (2013). To milliseconds and beyond: challenges in the simulation of protein folding. Curr. Opin. Struct. Biol. 23, 58-65. doi: 10. 1016/j. sbi. 2012. 11. 002.
    • (2013) Curr. Opin. Struct. Biol , vol.23 , pp. 58-65
    • Lane, T.J.1    Shukla, D.2    Beauchamp, K.A.3    Pande, V.S.4
  • 47
    • 70349560022 scopus 로고    scopus 로고
    • A combined solid-state NMR and MD characterization of the stability and dynamics of the HET-s(218-289) prion in its amyloid conformation
    • Lange, A., Gattin, Z., Van Melckebeke, H., Wasmer, C., Soragni, A., van Gunsteren, W. F., et al. (2009). A combined solid-state NMR and MD characterization of the stability and dynamics of the HET-s(218-289) prion in its amyloid conformation. Chembiochem 10, 1657-1665. doi: 10. 1002/cbic. 200900019.
    • (2009) Chembiochem , vol.10 , pp. 1657-1665
    • Lange, A.1    Gattin, Z.2    Van Melckebeke, H.3    Wasmer, C.4    Soragni, A.5    van Gunsteren, W.F.6
  • 48
    • 84867665458 scopus 로고    scopus 로고
    • Kinetic intermediates of amyloid fibrillation studied by hydrogen exchange methods with nuclear magnetic resonance
    • Lee, Y.-H., and Goto, Y. (2012). Kinetic intermediates of amyloid fibrillation studied by hydrogen exchange methods with nuclear magnetic resonance. Biochim. Biophys. Acta 1824, 1307-1323. doi: 10. 1016/j. bbapap. 2012. 07. 013.
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 1307-1323
    • Lee, Y.-H.1    Goto, Y.2
  • 49
    • 84857774493 scopus 로고    scopus 로고
    • Structure and dynamics of an unfolded protein examined by molecular dynamics simulation
    • Lindorff-Larsen, K., Trbovic, N., Maragakis, P., Piana, S., and Shaw, D. E. (2012). Structure and dynamics of an unfolded protein examined by molecular dynamics simulation. J. Am. Chem. Soc. 134, 3787-3791. doi: 10. 1021/ja209931w.
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 3787-3791
    • Lindorff-Larsen, K.1    Trbovic, N.2    Maragakis, P.3    Piana, S.4    Shaw, D.E.5
  • 50
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., and Szabo, A. (1982). Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104, 4546-4559. doi: 10. 1021/ja00381a009.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 51
    • 84901017485 scopus 로고    scopus 로고
    • Advantages of proteins being disordered
    • Liu, Z., and Huang, Y. (2014). Advantages of proteins being disordered. Protein Sci. 23, 539-550. doi: 10. 1002/pro. 2443.
    • (2014) Protein Sci , vol.23 , pp. 539-550
    • Liu, Z.1    Huang, Y.2
  • 52
    • 79960189344 scopus 로고    scopus 로고
    • Dynamic allostery: Linkers are not merely flexible
    • Ma, B., Tsai, C.-J., Haliloğlu, T., and Nussinov, R. (2011). Dynamic allostery: linkers are not merely flexible. Structure 19, 907-917. doi: 10. 1016/j. str. 2011. 06. 002.
    • (2011) Structure , vol.19 , pp. 907-917
    • Ma, B.1    Tsai, C.-J.2    Haliloğlu, T.3    Nussinov, R.4
  • 53
    • 84875472274 scopus 로고    scopus 로고
    • Solution NMR and computational methods for understanding protein allostery
    • Manley, G., Rivalta, I., and Loria, J. P. (2013). Solution NMR and computational methods for understanding protein allostery. J. Phys. Chem. B 117, 3063-3073. doi: 10. 1021/jp312576v.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 3063-3073
    • Manley, G.1    Rivalta, I.2    Loria, J.P.3
  • 54
    • 84867746731 scopus 로고    scopus 로고
    • Probing the diverse landscape of protein flexibility and binding
    • Marsh, J. A., Teichmann, S. A., and Forman-Kay, J. D. (2012). Probing the diverse landscape of protein flexibility and binding. Curr. Opin. Struct. Biol. 22, 643-650. doi: 10. 1016/j. sbi. 2012. 08. 008.
    • (2012) Curr. Opin. Struct. Biol , vol.22 , pp. 643-650
    • Marsh, J.A.1    Teichmann, S.A.2    Forman-Kay, J.D.3
  • 55
    • 84861181203 scopus 로고    scopus 로고
    • Allostery and binding cooperativity of the catalytic subunit of protein kinase A by NMR spectroscopy and molecular dynamics simulations
    • Masterson, L. R., Cembran, A., Shi, L., and Veglia, G. (2012). Allostery and binding cooperativity of the catalytic subunit of protein kinase A by NMR spectroscopy and molecular dynamics simulations. Adv. Protein Chem. Struct. Biol. 87, 363-389. doi: 10. 1016/B978-0-12-398312-1. 00012-3.
    • (2012) Adv. Protein Chem. Struct. Biol , vol.87 , pp. 363-389
    • Masterson, L.R.1    Cembran, A.2    Shi, L.3    Veglia, G.4
  • 56
    • 84891834552 scopus 로고    scopus 로고
    • Spontaneous aggregation of the insulin-derived steric zipper peptide VEALYL results in different aggregation forms with common features
    • Matthes, D., Daebel, V., Meyenberg, K., Riedel, D., Heim, G., Diederichsen, U., et al. (2014). Spontaneous aggregation of the insulin-derived steric zipper peptide VEALYL results in different aggregation forms with common features. J. Mol. Biol. 426, 362-376. doi: 10. 1016/j. jmb. 2013. 10. 020.
    • (2014) J. Mol. Biol , vol.426 , pp. 362-376
    • Matthes, D.1    Daebel, V.2    Meyenberg, K.3    Riedel, D.4    Heim, G.5    Diederichsen, U.6
  • 57
    • 79958826524 scopus 로고    scopus 로고
    • Protein dynamics and enzyme catalysis: Insights from simulations
    • McGeagh, J. D., Ranaghan, K. E., and Mulholland, A. J. (2011). Protein dynamics and enzyme catalysis: insights from simulations. Biochim. Biophys. Acta 1814, 1077-1092. doi: 10. 1016/j. bbapap. 2010. 12. 002.
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 1077-1092
    • McGeagh, J.D.1    Ranaghan, K.E.2    Mulholland, A.J.3
  • 58
    • 84901443611 scopus 로고    scopus 로고
    • Investigating the dynamic aspects of drug-protein recognition through a combination of MD and NMR analyses: Implications for the development of protein-protein interaction inhibitors
    • Meli, M., Pagano, K., Ragona, L., and Colombo, G. (2014). Investigating the dynamic aspects of drug-protein recognition through a combination of MD and NMR analyses: implications for the development of protein-protein interaction inhibitors. PLoS ONE 9: e97153. doi: 10. 1371/journal. pone. 0097153.
    • (2014) PLoS ONE , vol.9
    • Meli, M.1    Pagano, K.2    Ragona, L.3    Colombo, G.4
  • 59
    • 84898993517 scopus 로고    scopus 로고
    • The ensemble nature of allostery
    • Motlagh, H. N., Wrabl, J. O., Li, J., and Hilser, V. J. (2014). The ensemble nature of allostery. Nature 508, 331-339. doi: 10. 1038/nature13001.
    • (2014) Nature , vol.508 , pp. 331-339
    • Motlagh, H.N.1    Wrabl, J.O.2    Li, J.3    Hilser, V.J.4
  • 60
    • 84876554878 scopus 로고    scopus 로고
    • NMR as a tool to identify and characterize protein folding intermediates
    • Neira, J. L. (2013). NMR as a tool to identify and characterize protein folding intermediates. Arch. Biochem. Biophys. 531, 90-99. doi: 10. 1016/j. abb. 2012. 09. 003.
    • (2013) Arch. Biochem. Biophys , vol.531 , pp. 90-99
    • Neira, J.L.1
  • 61
    • 84860013075 scopus 로고    scopus 로고
    • Structure of an intermediate state in protein folding and aggregation
    • Neudecker, P., Robustelli, P., Cavalli, A., Walsh, P., Lundström, P., Zarrine-Afsar, A., et al. (2012). Structure of an intermediate state in protein folding and aggregation. Science 336, 362-366. doi: 10. 1126/science. 1214203.
    • (2012) Science , vol.336 , pp. 362-366
    • Neudecker, P.1    Robustelli, P.2    Cavalli, A.3    Walsh, P.4    Lundström, P.5    Zarrine-Afsar, A.6
  • 62
  • 63
    • 84893748547 scopus 로고    scopus 로고
    • The significance of the 2013 Nobel Prize in Chemistry and the challenges ahead
    • Nussinov, R. (2014). The significance of the 2013 Nobel Prize in Chemistry and the challenges ahead. PLoS Comput. Biol. 10: e1003423. doi: 10. 1371/journal. pcbi. 1003423.
    • (2014) PLoS Comput. Biol , vol.10
    • Nussinov, R.1
  • 64
    • 84856078561 scopus 로고    scopus 로고
    • Protein dynamics and conformational selection in bidirectional signal transduction
    • Nussinov, R., and Ma, B. (2012). Protein dynamics and conformational selection in bidirectional signal transduction. BMC Biol. 10: 2. doi: 10. 1186/1741-7007-10-2.
    • (2012) BMC Biol , vol.10
    • Nussinov, R.1    Ma, B.2
  • 65
    • 84883480131 scopus 로고    scopus 로고
    • Allosteric conformational barcodes direct signaling in the cell
    • Nussinov, R., Ma, B., Tsai, C.-J., and Csermely, P. (2013). Allosteric conformational barcodes direct signaling in the cell. Structure 21, 1509-1521. doi: 10. 1016/j. str. 2013. 06. 002.
    • (2013) Structure , vol.21 , pp. 1509-1521
    • Nussinov, R.1    Ma, B.2    Tsai, C.-J.3    Csermely, P.4
  • 66
    • 84876266689 scopus 로고    scopus 로고
    • Allostery in disease and in drug discovery
    • Nussinov, R., and Tsai, C. (2013). Allostery in disease and in drug discovery. Cell 153, 293-305. doi: 10. 1016/j. cell. 2013. 03. 034.
    • (2013) Cell , vol.153 , pp. 293-305
    • Nussinov, R.1    Tsai, C.2
  • 67
    • 84897052340 scopus 로고    scopus 로고
    • Free energy diagrams for protein function
    • Nussinov, R., and Tsai, C.-J. (2014a). Free energy diagrams for protein function. Chem. Biol. 21, 311-318. doi: 10. 1016/j. chembiol. 2013. 12. 015.
    • (2014) Chem. Biol , vol.21 , pp. 311-318
    • Nussinov, R.1    Tsai, C.-J.2
  • 68
    • 84899656717 scopus 로고    scopus 로고
    • Unraveling structural mechanisms of allosteric drug action
    • Nussinov, R., and Tsai, C.-J. (2014b). Unraveling structural mechanisms of allosteric drug action. Trends Pharmacol. Sci. 35, 256-264. doi: 10. 1016/j. tips. 2014. 03. 006.
    • (2014) Trends Pharmacol. Sci , vol.35 , pp. 256-264
    • Nussinov, R.1    Tsai, C.-J.2
  • 69
    • 84920842453 scopus 로고    scopus 로고
    • The design of covalent allosteric drugs
    • Nussinov, R., and Tsai, C.-J. (2015). The design of covalent allosteric drugs. Annu. Rev. Pharmacol. Toxicol. 55, 249-267. doi: 10. 1146/annurev-pharmtox-010814-124401.
    • (2015) Annu. Rev. Pharmacol. Toxicol , vol.55 , pp. 249-267
    • Nussinov, R.1    Tsai, C.-J.2
  • 70
    • 84867745578 scopus 로고    scopus 로고
    • Functional dynamics of proteins revealed by solution NMR
    • Osawa, M., Takeuchi, K., Ueda, T., Nishida, N., and Shimada, I. (2012). Functional dynamics of proteins revealed by solution NMR. Curr. Opin. Struct. Biol. 22, 660-669. doi: 10. 1016/j. sbi. 2012. 08. 007.
    • (2012) Curr. Opin. Struct. Biol , vol.22 , pp. 660-669
    • Osawa, M.1    Takeuchi, K.2    Ueda, T.3    Nishida, N.4    Shimada, I.5
  • 71
    • 84892500140 scopus 로고    scopus 로고
    • Exploring the minimally frustrated energy landscape of unfolded ACBP
    • Ozenne, V., Noel, J. K., Heidarsson, P. O., Brander, S., Poulsen, F. M., Jensen, M. R., et al. (2014). Exploring the minimally frustrated energy landscape of unfolded ACBP. J. Mol. Biol. 426, 722-734. doi: 10. 1016/j. jmb. 2013. 10. 031.
    • (2014) J. Mol. Biol , vol.426 , pp. 722-734
    • Ozenne, V.1    Noel, J.K.2    Heidarsson, P.O.3    Brander, S.4    Poulsen, F.M.5    Jensen, M.R.6
  • 72
    • 84878943828 scopus 로고    scopus 로고
    • Transient access to the protein interior: Simulation versus NMR
    • Persson, F., and Halle, B. (2013). Transient access to the protein interior: simulation versus NMR. J. Am. Chem. Soc. 135, 8735-8748. doi: 10. 1021/ja403405d.
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 8735-8748
    • Persson, F.1    Halle, B.2
  • 73
    • 84892963298 scopus 로고    scopus 로고
    • Assessing the accuracy of physical models used in protein-folding simulations: Quantitative evidence from long molecular dynamics simulations
    • Piana, S., Klepeis, J. L., and Shaw, D. E. (2014). Assessing the accuracy of physical models used in protein-folding simulations: quantitative evidence from long molecular dynamics simulations. Curr. Opin. Struct. Biol. 24, 98-105. doi: 10. 1016/j. sbi. 2013. 12. 006.
    • (2014) Curr. Opin. Struct. Biol , vol.24 , pp. 98-105
    • Piana, S.1    Klepeis, J.L.2    Shaw, D.E.3
  • 74
    • 84884284595 scopus 로고    scopus 로고
    • Fast real-time NMR methods for characterizing short-lived molecular states
    • Rennella, E., and Brutscher, B. (2013). Fast real-time NMR methods for characterizing short-lived molecular states. Chemphyschem 14, 3059-3070. doi: 10. 1002/cphc. 201300339.
    • (2013) Chemphyschem , vol.14 , pp. 3059-3070
    • Rennella, E.1    Brutscher, B.2
  • 76
    • 84902962134 scopus 로고    scopus 로고
    • How fast is your camera? Timescales for molecular motion and their role in restraining molecular dynamics
    • Romo, T. D., and Grossfield, A. (2014). How fast is your camera? Timescales for molecular motion and their role in restraining molecular dynamics. Biophys. J. 106, 2549-2551. doi: 10. 1016/j. bpj. 2014. 05. 022.
    • (2014) Biophys. J , vol.106 , pp. 2549-2551
    • Romo, T.D.1    Grossfield, A.2
  • 77
    • 84862676450 scopus 로고    scopus 로고
    • Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics
    • Salmon, L., Pierce, L., Grimm, A., Ortega Roldan, J.-L., Mollica, L., Jensen, M. R., et al. (2012). Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics. Angew. Chem. 51, 6103-6106. doi: 10. 1002/anie. 201202026.
    • (2012) Angew. Chem , vol.51 , pp. 6103-6106
    • Salmon, L.1    Pierce, L.2    Grimm, A.3    Ortega Roldan, J.-L.4    Mollica, L.5    Jensen, M.R.6
  • 79
    • 77957937199 scopus 로고    scopus 로고
    • Atomic-level characterization of the structural dynamics of proteins
    • Shaw, D. E., Maragakis, P., Lindorff-Larsen, K., Piana, S., Dror, R. O., Eastwood, M. P., et al. (2010). Atomic-level characterization of the structural dynamics of proteins. Science 330, 341-346. doi: 10. 1126/science. 1187409.
    • (2010) Science , vol.330 , pp. 341-346
    • Shaw, D.E.1    Maragakis, P.2    Lindorff-Larsen, K.3    Piana, S.4    Dror, R.O.5    Eastwood, M.P.6
  • 80
    • 84899711683 scopus 로고    scopus 로고
    • Discrete molecular dynamics can predict helical prestructured motifs in disordered proteins
    • Szöllosi, D., Horváth, T., Han, K. H., Dokholyan, N. V., Tompa, P., Kalmár, L., et al. (2014). Discrete molecular dynamics can predict helical prestructured motifs in disordered proteins. PLoS ONE 9: e95795. doi: 10. 1371/journal. pone. 0095795.
    • (2014) PLoS ONE , vol.9
    • Szöllosi, D.1    Horváth, T.2    Han, K.H.3    Dokholyan, N.V.4    Tompa, P.5    Kalmár, L.6
  • 81
    • 79958774937 scopus 로고    scopus 로고
    • Protein stability, flexibility and function
    • Teilum, K., Olsen, J. G., and Kragelund, B. B. (2011). Protein stability, flexibility and function. Biochim. Biophys. Acta 1814, 969-976. doi: 10. 1016/j. bbapap. 2010. 11. 005.
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 969-976
    • Teilum, K.1    Olsen, J.G.2    Kragelund, B.B.3
  • 82
    • 84859910826 scopus 로고    scopus 로고
    • Understanding protein unfolding from molecular simulations
    • Toofanny, R. D., and Daggett, V. (2012). Understanding protein unfolding from molecular simulations. Wiley Interdiscip. Rev. Comput. Mol. Sci. 2, 405-423. doi: 10. 1002/wcms. 1088.
    • (2012) Wiley Interdiscip. Rev. Comput. Mol. Sci , vol.2 , pp. 405-423
    • Toofanny, R.D.1    Daggett, V.2
  • 84
    • 84895745240 scopus 로고    scopus 로고
    • A unified view of "how allostery works. "
    • Tsai, C.-J., and Nussinov, R. (2014). A unified view of "how allostery works. " PLoS Comput. Biol. 10: e1003394. doi: 10. 1371/journal. pcbi. 1003394.
    • (2014) PLoS Comput. Biol , vol.10
    • Tsai, C.-J.1    Nussinov, R.2
  • 85
    • 84926317610 scopus 로고    scopus 로고
    • Wrecked regulation of intrinsically disordered proteins in diseases: Pathogenicity of deregulated regulators
    • Uversky, V. N. (2014). Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators. Front. Mol. Biosci. 1: 6. doi: 10. 3389/fmolb. 2014. 00006.
    • (2014) Front. Mol. Biosci , vol.1
    • Uversky, V.N.1
  • 87
    • 84875470470 scopus 로고    scopus 로고
    • Protein self-assembly intermediates
    • Vendruscolo, M., and Dobson, C. M. (2013). Protein self-assembly intermediates. Nat. Chem. Biol. 9, 216-217. doi: 10. 1038/nchembio. 1210.
    • (2013) Nat. Chem. Biol , vol.9 , pp. 216-217
    • Vendruscolo, M.1    Dobson, C.M.2
  • 88
    • 84895918624 scopus 로고    scopus 로고
    • Evidence against the "Y-T coupling" mechanism of activation in the response regulator NtrC
    • Villali, J., Pontiggia, F., Clarkson, M. W., Hagan, M. F., and Kern, D. (2014). Evidence against the "Y-T coupling" mechanism of activation in the response regulator NtrC. J. Mol. Biol. 426, 1554-1567. doi: 10. 1016/j. jmb. 2013. 12. 027.
    • (2014) J. Mol. Biol , vol.426 , pp. 1554-1567
    • Villali, J.1    Pontiggia, F.2    Clarkson, M.W.3    Hagan, M.F.4    Kern, D.5
  • 89
    • 84873526287 scopus 로고    scopus 로고
    • The dark energy of proteins comes to light: Conformational entropy and its role in protein function revealed by NMR relaxation
    • Wand, A. J. (2013). The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation. Curr. Opin. Struct. Biol. 23, 75-81. doi: 10. 1016/j. sbi. 2012. 11. 005.
    • (2013) Curr. Opin. Struct. Biol , vol.23 , pp. 75-81
    • Wand, A.J.1
  • 90
    • 84922988123 scopus 로고    scopus 로고
    • Conformational selection in protein binding and function
    • Weikl, T. R., and Paul, F. (2014). Conformational selection in protein binding and function. Protein Sci. 23, 1508-1518. doi: 10. 1002/pro. 2539.
    • (2014) Protein Sci , vol.23 , pp. 1508-1518
    • Weikl, T.R.1    Paul, F.2
  • 91
    • 84925114160 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in cellular signalling and regulation
    • Wright, P. E., and Dyson, H. J. (2014). Intrinsically disordered proteins in cellular signalling and regulation. Nat. Rev. Mol. Cell Biol. 16, 18-29. doi: 10. 1038/nrm3920.
    • (2014) Nat. Rev. Mol. Cell Biol , vol.16 , pp. 18-29
    • Wright, P.E.1    Dyson, H.J.2
  • 92
    • 84879184332 scopus 로고    scopus 로고
    • NMR relaxation in proteins with fast internal motions and slow conformational exchange: Model-free framework and Markov state simulations
    • Xia, J., Deng, N., and Levy, R. M. (2013). NMR relaxation in proteins with fast internal motions and slow conformational exchange: model-free framework and Markov state simulations. J. Phys. Chem. B 117, 6625-6634. doi: 10. 1021/jp400797y.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 6625-6634
    • Xia, J.1    Deng, N.2    Levy, R.M.3
  • 93
    • 84908062585 scopus 로고    scopus 로고
    • Visualizing an ultra-weak protein-protein interaction in phosphorylation signaling
    • Xing, Q., Huang, P., Yang, J., Sun, J., Gong, Z., Dong, X., et al. (2014). Visualizing an ultra-weak protein-protein interaction in phosphorylation signaling. Angew. Chem. 126, 11685-11689. doi: 10. 1002/ange. 201405976.
    • (2014) Angew. Chem , vol.126 , pp. 11685-11689
    • Xing, Q.1    Huang, P.2    Yang, J.3    Sun, J.4    Gong, Z.5    Dong, X.6
  • 94
    • 84856728860 scopus 로고    scopus 로고
    • Microsecond time-scale conformational exchange in proteins: Using long molecular dynamics trajectory to simulate NMR relaxation dispersion data
    • Xue, Y., Ward, J. M., Yuwen, T., Podkorytov, I. S., and Skrynnikov, N. R. (2012). Microsecond time-scale conformational exchange in proteins: using long molecular dynamics trajectory to simulate NMR relaxation dispersion data. J. Am. Chem. Soc. 134, 2555-2562. doi: 10. 1021/ja206442c.
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 2555-2562
    • Xue, Y.1    Ward, J.M.2    Yuwen, T.3    Podkorytov, I.S.4    Skrynnikov, N.R.5
  • 95
    • 84872283908 scopus 로고    scopus 로고
    • Analysis of 15N-1H NMR relaxation in proteins by a combined experimental and molecular dynamics simulation approach: Picosecond-nanosecond dynamics of the Rho GTPase binding domain of plexin-B1 in the dimeric state indicates allosteric pathways
    • Zerbetto, M., Anderson, R., Bouguet-Bonnet, S., Rech, M., Zhang, L., Meirovitch, E., et al. (2013). Analysis of 15N-1H NMR relaxation in proteins by a combined experimental and molecular dynamics simulation approach: picosecond-nanosecond dynamics of the Rho GTPase binding domain of plexin-B1 in the dimeric state indicates allosteric pathways. J. Phys. Chem. B 117, 174-184. doi: 10. 1021/jp310142f.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 174-184
    • Zerbetto, M.1    Anderson, R.2    Bouguet-Bonnet, S.3    Rech, M.4    Zhang, L.5    Meirovitch, E.6
  • 96
    • 84893369497 scopus 로고    scopus 로고
    • Theoretical frameworks for multiscale modeling and simulation
    • Zhou, H.-X. (2014). Theoretical frameworks for multiscale modeling and simulation. Curr. Opin. Struc. Biol. 25C, 67-76. doi: 10. 1016/j. sbi. 2014. 01. 004.
    • (2014) Curr. Opin. Struc. Biol , vol.25 C , pp. 67-76
    • Zhou, H.-X.1


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