메뉴 건너뛰기




Volumn 118, Issue 47, 2014, Pages 13468-13476

Long-range conformational transition of a photoswitchable allosteric protein: Molecular dynamics simulation study

Author keywords

[No Author keywords available]

Indexed keywords

NON RECEPTOR PROTEIN TYROSINE PHOSPHATASE 13; PTPN13 PROTEIN, HUMAN; WATER;

EID: 84914161401     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp506873y     Document Type: Article
Times cited : (25)

References (70)
  • 1
    • 84876266689 scopus 로고    scopus 로고
    • Allostery in Disease and in Drug Discovery
    • Nussinov, R.; Tsai, C.-J. Allostery in Disease and in Drug Discovery Cell 2013, 153, 293-305
    • (2013) Cell , vol.153 , pp. 293-305
    • Nussinov, R.1    Tsai, C.-J.2
  • 3
    • 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
  • 4
    • 48249141040 scopus 로고    scopus 로고
    • Allostery and Cooperativity Revisited
    • Cui, Q.; Karplus, M. Allostery and Cooperativity Revisited Protein Sci. 2008, 17, 1295-1307
    • (2008) Protein Sci. , vol.17 , pp. 1295-1307
    • Cui, Q.1    Karplus, M.2
  • 5
    • 0021658956 scopus 로고
    • Allostery without Conformational Change: A Plausible Model
    • Cooper, A.; Dryden, D. Allostery without Conformational Change: A Plausible Model Eur. Biophys. J. Biophys. Lett. 1984, 11, 103-109
    • (1984) Eur. Biophys. J. Biophys. Lett. , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.2
  • 6
    • 0346220393 scopus 로고    scopus 로고
    • The Role of Dynamics in Allosteric Regulation
    • Kern, D.; Zuiderweg, E. The Role of Dynamics in Allosteric Regulation Curr. Opin. Struct. Biol. 2003, 13, 748-757
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 748-757
    • Kern, D.1    Zuiderweg, E.2
  • 7
    • 33748363077 scopus 로고    scopus 로고
    • Kalodimos, Dynamically Driven Protein Allostery
    • Popovych, N.; Sun, S.; Ebright, R. Kalodimos, Dynamically Driven Protein Allostery Nat. Struct. Mol. Biol. 2006, 13, 831-838
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 831-838
    • Popovych, N.1    Sun, S.2    Ebright, R.3
  • 8
    • 34447503697 scopus 로고    scopus 로고
    • Conformational Entropy in Molecular Recognition by Proteins
    • Frederick, K. K.; Marlow, M. S.; Valentine, K. G.; Wand, A. J. Conformational Entropy in Molecular Recognition by Proteins Nature 2007, 448, 325-329
    • (2007) Nature , vol.448 , pp. 325-329
    • Frederick, K.K.1    Marlow, M.S.2    Valentine, K.G.3    Wand, A.J.4
  • 9
    • 64849111005 scopus 로고    scopus 로고
    • Sending Signal Dynamically
    • Smock, R. G.; Gierasch, L. M. Sending Signal Dynamically Science 2009, 324, 198-203
    • (2009) Science , vol.324 , pp. 198-203
    • Smock, R.G.1    Gierasch, L.M.2
  • 10
    • 47349099470 scopus 로고    scopus 로고
    • Mapping of Two Networks of Residues that Exhibit Structural and Dynamical Changes upon Binding in a PDZ Domain Protein
    • Dhulesia, A.; Gsponer, J.; Vendruscolo, M. Mapping of Two Networks of Residues that Exhibit Structural and Dynamical Changes upon Binding in a PDZ Domain Protein J. Am. Chem. Soc. 2008, 130, 8931-8939
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 8931-8939
    • Dhulesia, A.1    Gsponer, J.2    Vendruscolo, M.3
  • 11
    • 0347753736 scopus 로고    scopus 로고
    • Ligand-Dependent Dynamics and Intramolecular Signaling in a PDZ Domain
    • Fuentes, E.; Der, C.; Lee, A. Ligand-Dependent Dynamics and Intramolecular Signaling in a PDZ Domain J. Mol. Biol. 2004, 335, 1105-1115
    • (2004) J. Mol. Biol. , vol.335 , pp. 1105-1115
    • Fuentes, E.1    Der, C.2    Lee, A.3
  • 12
    • 33750795402 scopus 로고    scopus 로고
    • Evaluation of Energetic and Dynamic Coupling Networks in a PDZ Domain Protein
    • Fuentes, E. J.; Gilmore, S. A.; Mauldin, R. V.; Lee, A. L. Evaluation of Energetic and Dynamic Coupling Networks in a PDZ Domain Protein J. Mol. Biol. 2006, 364, 337-351
    • (2006) J. Mol. Biol. , vol.364 , pp. 337-351
    • Fuentes, E.J.1    Gilmore, S.A.2    Mauldin, R.V.3    Lee, A.L.4
  • 14
    • 84870707533 scopus 로고    scopus 로고
    • Accurate Prediction of the Dynamical Changes within the Second PDZ Domain of PTP1e
    • Cilia, E.; Vuister, G. W.; Lenaerts, T. Accurate Prediction of the Dynamical Changes within the Second PDZ Domain of PTP1e. PLoS Comput. Biol. 2012, 8.
    • (2012) PLoS Comput. Biol. , vol.8
    • Cilia, E.1    Vuister, G.W.2    Lenaerts, T.3
  • 15
    • 0030604722 scopus 로고    scopus 로고
    • Crystal Structures of a Complexed and Peptide-Free Membrane Protein-Binding Domain: Molecular Basis of Peptide Recognition by PDZ
    • Doyle, D.; Lee, A.; Lewis, J.; Kim, E.; Sheng, M.; MacKinnon, R. Crystal Structures of a Complexed and Peptide-Free Membrane Protein-Binding Domain: Molecular Basis of Peptide Recognition by PDZ Cell 1996, 85, 1067-1076
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 16
    • 78049307619 scopus 로고    scopus 로고
    • Crystallographic and Nuclear Magnetic Resonance Evaluation of the Impact of Peptide Binding to the Second PDZ Domain of Protein Tyrosine Phosphatase 1E
    • Zhang, J.; Sapienza, P. J.; Ke, H.; Chang, A.; Hengel, S. R.; Wang, H.; Phillips, G. N., Jr.; Lee, A. L. Crystallographic and Nuclear Magnetic Resonance Evaluation of the Impact of Peptide Binding to the Second PDZ Domain of Protein Tyrosine Phosphatase 1E Biochemistry 2010, 49, 9280-9291
    • (2010) Biochemistry , vol.49 , pp. 9280-9291
    • Zhang, J.1    Sapienza, P.J.2    Ke, H.3    Chang, A.4    Hengel, S.R.5    Wang, H.6    Phillips, G.N.7    Lee, A.L.8
  • 18
    • 0034740693 scopus 로고    scopus 로고
    • Mechanism and Role of PDZ Domains in Signaling Complex Assembly
    • Harris, B.; Lim, W. Mechanism and Role of PDZ Domains in Signaling Complex Assembly J. Cell Sci. 2001, 114, 3219-3231
    • (2001) J. Cell Sci. , vol.114 , pp. 3219-3231
    • Harris, B.1    Lim, W.2
  • 19
  • 20
    • 77952705907 scopus 로고    scopus 로고
    • PDZ Domains and their Binding Partners: Structure, Specificity, and Modification
    • Lee, H.-J.; Zheng, J. J. PDZ Domains and their Binding Partners: Structure, Specificity, and Modification. Cell Commun. Signal. 2010, 8.
    • (2010) Cell Commun. Signal. , vol.8
    • Lee, H.-J.1    Zheng, J.J.2
  • 22
    • 67650032475 scopus 로고    scopus 로고
    • Energy Flow and Long-Range Correlations in Guanine-Binding Riboswitch: A Nonequilibrium Molecular Dynamics Study
    • Nguyen, P. H.; Derreumaux, P.; Stock, G. Energy Flow and Long-Range Correlations in Guanine-Binding Riboswitch: A Nonequilibrium Molecular Dynamics Study J. Phys. Chem. B 2009, 113, 9340-9347
    • (2009) J. Phys. Chem. B , vol.113 , pp. 9340-9347
    • Nguyen, P.H.1    Derreumaux, P.2    Stock, G.3
  • 23
    • 77955505542 scopus 로고    scopus 로고
    • Spontaneous Quaternary and Tertiary T-R Transitions of Human Hemoglobin in Molecular Dynamics Simulation
    • Hub, J. S.; Kubitzki, M.; de Groot, B. L. Spontaneous Quaternary and Tertiary T-R Transitions of Human Hemoglobin in Molecular Dynamics Simulation PLoS Comput. Biol. 2010, 6, e1000774
    • (2010) PLoS Comput. Biol. , vol.6 , pp. 1000774
    • Hub, J.S.1    Kubitzki, M.2    De Groot, B.L.3
  • 24
    • 80051867711 scopus 로고    scopus 로고
    • Communication Maps Computed for Homodimeric Hemoglobin: Computational Study of Water-Mediated Energy Transport in Proteins
    • Gnanasekaran, R.; Agbo, J. K.; Leitner, D. M. Communication Maps Computed for Homodimeric Hemoglobin: Computational Study of Water-Mediated Energy Transport in Proteins J. Chem. Phys. 2011, 135, 065103
    • (2011) J. Chem. Phys. , vol.135 , pp. 065103
    • Gnanasekaran, R.1    Agbo, J.K.2    Leitner, D.M.3
  • 25
    • 79953100071 scopus 로고    scopus 로고
    • Simulations of Allosteric Transitions
    • Elber, R. Simulations of Allosteric Transitions Curr. Opin. Struct. Biol. 2011, 21, 167-172
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 167-172
    • Elber, R.1
  • 26
    • 84884688109 scopus 로고    scopus 로고
    • Collective Dynamics Underlying Allosteric Transitions in Hemoglobin
    • Vesper, M. D.; de Groot, B. L. Collective Dynamics Underlying Allosteric Transitions in Hemoglobin PLoS Comp. Biol. 2013, 9, e1003232
    • (2013) PLoS Comp. Biol. , vol.9 , pp. 1003232
    • Vesper, M.D.1    De Groot, B.L.2
  • 27
    • 84887037245 scopus 로고    scopus 로고
    • Allostery without Conformational Change: Modelling Protein Dynamics at Multiple Scales
    • McLeish, T. C. B.; Rodgers, T. L.; Wilson, M. R. Allostery without Conformational Change: Modelling Protein Dynamics at Multiple Scales Phys. Biol. 2013, 10, 056004
    • (2013) Phys. Biol. , vol.10 , pp. 056004
    • McLeish, T.C.B.1    Rodgers, T.L.2    Wilson, M.R.3
  • 28
    • 84884546753 scopus 로고    scopus 로고
    • Modulation of Global Low-Frequency Motions Underlies Allosteric Regulation: Demonstration in CRP/FNR Family Transcription Factors
    • Rodgers, T. L.; Townsend, P. D.; Burnell, D.; Jones, M. L.; Richards, S. A.; McLeish, T. C. B.; Pohl, E.; Wilson, M. R.; Cann, M. J. Modulation of Global Low-Frequency Motions Underlies Allosteric Regulation: Demonstration in CRP/FNR Family Transcription Factors PLoS Biol. 2013, 11, e1001651
    • (2013) PLoS Biol. , vol.11 , pp. 1001651
    • Rodgers, T.L.1    Townsend, P.D.2    Burnell, D.3    Jones, M.L.4    Richards, S.A.5    McLeish, T.C.B.6    Pohl, E.7    Wilson, M.R.8    Cann, M.J.9
  • 29
    • 84896778565 scopus 로고    scopus 로고
    • Allosteric Control of Kinesin’s Motor Domain by Tubulin: A Molecular Dynamics Study
    • Krukau, A.; Knecht, V.; Lipowsky, R. Allosteric Control of Kinesin’s Motor Domain by Tubulin: A Molecular Dynamics Study Phys. Chem. Chem. Phys. 2014, 16, 6189-6198
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , pp. 6189-6198
    • Krukau, A.1    Knecht, V.2    Lipowsky, R.3
  • 30
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families
    • Lockless, S. W.; Ranganathan, R. Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families Science 1999, 286, 295-299
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 32
    • 22444450449 scopus 로고    scopus 로고
    • Intramolecular Signaling Pathways Revealed by Molecular Anisotropic Thermal Diffusion
    • Ota, N.; Agard, D. A. Intramolecular Signaling Pathways Revealed by Molecular Anisotropic Thermal Diffusion J. Mol. Biol. 2005, 351, 345-354
    • (2005) J. Mol. Biol. , vol.351 , pp. 345-354
    • Ota, N.1    Agard, D.A.2
  • 33
    • 33749029273 scopus 로고    scopus 로고
    • Pump-Probe Molecular Dynamics as a Tool for Studying Protein Motion and Long Range Coupling
    • Sharp, K.; Skinner, J. J. Pump-Probe Molecular Dynamics as a Tool for Studying Protein Motion and Long Range Coupling Proteins 2006, 65, 347-361
    • (2006) Proteins , vol.65 , pp. 347-361
    • Sharp, K.1    Skinner, J.J.2
  • 34
    • 58949102247 scopus 로고    scopus 로고
    • Signaling Pathways of PDZ2 Domain: A Molecular Dynamics Interaction Correlation Analysis
    • Kong, Y.; Karplus, M. Signaling Pathways of PDZ2 Domain: A Molecular Dynamics Interaction Correlation Analysis Proteins 2009, 74, 145-154
    • (2009) Proteins , vol.74 , pp. 145-154
    • Kong, Y.1    Karplus, M.2
  • 35
    • 78649883885 scopus 로고    scopus 로고
    • Interaction Energy Based Protein Structure Networks
    • S.Vijayabaskar, M.; Vishveshwara, S. Interaction Energy Based Protein Structure Networks Biophys. J. 2010, 99, 3704-3715
    • (2010) Biophys. J. , vol.99 , pp. 3704-3715
    • Vijayabaskar, M.S.1    Vishveshwara, S.2
  • 37
    • 70450065485 scopus 로고    scopus 로고
    • Identification of Specificity and Promiscuity of PDZ Domain Interactions through their Dynamic Behavior
    • Gerek, Z. N.; Keskin, O.; Ozkan, S. B. Identification of Specificity and Promiscuity of PDZ Domain Interactions through their Dynamic Behavior Proteins 2009, 77, 796-811
    • (2009) Proteins , vol.77 , pp. 796-811
    • Gerek, Z.N.1    Keskin, O.2    Ozkan, S.B.3
  • 38
    • 80055066238 scopus 로고    scopus 로고
    • Change in Allosteric Network Affects Binding Affinities of PDZ Domains: Analysis through Perturbation Response Scanning
    • Gerek, Z. N.; Ozkan, S. B. Change in Allosteric Network Affects Binding Affinities of PDZ Domains: Analysis through Perturbation Response Scanning PLoS Comput. Biol. 2011, 7, e1002154
    • (2011) PLoS Comput. Biol. , vol.7 , pp. 1002154
    • Gerek, Z.N.1    Ozkan, S.B.2
  • 39
    • 84863939894 scopus 로고    scopus 로고
    • Equilibrium Fluctuations of a Single Folded Protein Reveal a Multitude of Potential Cryptic Allosteric Sites
    • Bowman, G. R.; Geissler, P. L. Equilibrium Fluctuations of a Single Folded Protein Reveal a Multitude of Potential Cryptic Allosteric Sites Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 11681-11686
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 11681-11686
    • Bowman, G.R.1    Geissler, P.L.2
  • 40
    • 73449144096 scopus 로고    scopus 로고
    • Dynamic Allostery in the Methionine Repressor Revealed by Force Distribution Analysis
    • Stacklies, W.; Xia, F.; Gräter, F. Dynamic Allostery in the Methionine Repressor Revealed by Force Distribution Analysis PLoS Comput. Biol. 2009, 5 (e1000574) 11
    • (2009) PLoS Comput. Biol. , vol.5 , pp. 11
    • Stacklies, W.1    Xia, F.2    Gräter, F.3
  • 41
    • 34848882812 scopus 로고    scopus 로고
    • Signal Propagation in Proteins and Relation to Equilibrium Fluctuations
    • Chennubhotla, C.; Bahar, I. Signal Propagation in Proteins and Relation to Equilibrium Fluctuations PloS Comput. Biol. 2007, 9 (e172) 1716-1726
    • (2007) PloS Comput. Biol. , vol.9 , pp. 1716-1726
    • Chennubhotla, C.1    Bahar, I.2
  • 42
    • 84856514490 scopus 로고    scopus 로고
    • Detection of Allosteric Signal Transmission by Information-Theoretic Analysis of Protein Dynamics
    • Pandini, A.; Fornili, A.; Fraternali, F.; Kleinjung, J. Detection of Allosteric Signal Transmission by Information-Theoretic Analysis of Protein Dynamics FASEB J. 2012, 26, 868-881
    • (2012) FASEB J. , vol.26 , pp. 868-881
    • Pandini, A.1    Fornili, A.2    Fraternali, F.3    Kleinjung, J.4
  • 43
    • 84901660019 scopus 로고    scopus 로고
    • NbIT: A New Information Theory-Based Analysis of Allosteric Mechanisms Reveals Residues that Underlie Function in the Leucine Transporter LeuT
    • LeVine, M. V.; Weinstein, H. NbIT: A New Information Theory-Based Analysis of Allosteric Mechanisms Reveals Residues that Underlie Function in the Leucine Transporter LeuT PLoS Comput. Biol. 2014, 10, e1003603
    • (2014) PLoS Comput. Biol. , vol.10 , pp. 1003603
    • Levine, M.V.1    Weinstein, H.2
  • 46
    • 33745294757 scopus 로고    scopus 로고
    • Azobenzene as Conformational Switch in Model Peptides
    • Renner, C.; Moroder, L. Azobenzene as Conformational Switch in Model Peptides Chem. Biol. Chem. 2006, 7, 869-878
    • (2006) Chem. Biol. Chem. , vol.7 , pp. 869-878
    • Renner, C.1    Moroder, L.2
  • 50
    • 80455127006 scopus 로고    scopus 로고
    • Real Time Observation of Ultrafast Peptide Conformational Dynamics: MD Simulation vs. IR Experiment
    • Nguyen, P. H.; Staudt, H.; Wachtveitl, J.; Stock, G. Real Time Observation of Ultrafast Peptide Conformational Dynamics: MD Simulation vs. IR Experiment J. Phys. Chem. B 2011, 115, 13084-13092
    • (2011) J. Phys. Chem. B , vol.115 , pp. 13084-13092
    • Nguyen, P.H.1    Staudt, H.2    Wachtveitl, J.3    Stock, G.4
  • 51
    • 84875592758 scopus 로고    scopus 로고
    • GROMACS 4.5: A High-Throughput and Highly Parallel Open Source Molecular Simulation Toolkit
    • Pronk GROMACS 4.5: a High-Throughput and Highly Parallel Open Source Molecular Simulation Toolkit Bioinformatics 2013, 29, 845-854
    • (2013) Bioinformatics , vol.29 , pp. 845-854
    • Pronk1
  • 52
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of Multiple Amber Force Fields and Development of Improved Protein Backbone Parameters
    • Hornak, V.; Abel, R.; Okur, A.; Strockbine, B.; Roitberg, A.; Simmerling, C. Comparison of Multiple Amber Force Fields and Development of Improved Protein Backbone Parameters Proteins 2006, 65, 712-725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 53
    • 67649494492 scopus 로고    scopus 로고
    • Optimized Molecular Dynamics Force Fields Applied to the Helix-Coil Transition of Polypeptides
    • Best, R. B.; Hummer, G. Optimized Molecular Dynamics Force Fields Applied to the Helix-Coil Transition of Polypeptides J. Phys. Chem. B 2009, 113, 9004-9015
    • (2009) J. Phys. Chem. B , vol.113 , pp. 9004-9015
    • Best, R.B.1    Hummer, G.2
  • 56
    • 49449085241 scopus 로고    scopus 로고
    • Determination of Alkali and Halide Monovalent Ion Parameters for Use in Explicitly Solvated Biomolecular Simulations
    • Joung, I. S.; Cheatham, T. E., III Determination of Alkali and Halide Monovalent Ion Parameters for Use in Explicitly Solvated Biomolecular Simulations J. Phys. Chem. B 2008, 112, 9020-9041
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9020-9041
    • Joung, I.S.1    Cheatham, E.T.2
  • 57
    • 70450206724 scopus 로고    scopus 로고
    • revision A.1; Gaussian Inc: Wallingford, CT.
    • Frisch, M. J. Gaussian 09, revision A.1; Gaussian Inc: Wallingford, CT, 2009.
    • (2009) Gaussian 09
    • Frisch, M.J.1
  • 58
    • 3042524904 scopus 로고
    • A Well-Behaved Electrostatic Potential Based Method Using Charge Restraints for Deriving Atomic Charges: The RESP Model
    • Bayly, C. I.; Cieplak, P.; Cornell, W. D.; Kollman, P. A. A Well-Behaved Electrostatic Potential Based Method Using Charge Restraints for Deriving Atomic Charges: The RESP Model J. Phys. Chem. 1993, 97, 10269-10280
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 59
    • 33645200462 scopus 로고    scopus 로고
    • Antechamber, An Accessory Software Package for Molecular Mechanical Calculations
    • Wang, J.; Wang, W.; Kollman, P. A.; Case, D. A. Antechamber, An Accessory Software Package for Molecular Mechanical Calculations J. Comput. Chem. 2005, 25, 1157-1174
    • (2005) J. Comput. Chem. , vol.25 , pp. 1157-1174
    • Wang, J.1    Wang, W.2    Kollman, P.A.3    Case, D.A.4
  • 60
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess, B.; Kutzner, C.; van der Spoel, D.; Lindahl, E. GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation J. Chem. Theor. Comp. 2008, 4, 435-447
    • (2008) J. Chem. Theor. Comp. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 61
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) Method for Ewald Sums in Large Systems
    • Darden, T.; York, D.; Petersen, L. Particle mesh Ewald: An N log(N) Method for Ewald Sums in Large Systems J. Chem. Phys. 1993, 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Petersen, L.3
  • 62
    • 33846086933 scopus 로고    scopus 로고
    • Canonical Sampling through Velocity Rescaling
    • Bussi, G.; Donadio, D.; Parrinello, M. Canonical Sampling through Velocity Rescaling J. Chem. Phys. 2007, 126, 0141011-0141017
    • (2007) J. Chem. Phys. , vol.126 , pp. 0141011-0141017
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 64
    • 68349093958 scopus 로고    scopus 로고
    • TALOS Plus: A Hybrid Method for Predicting Protein Torsion Angles from NMR Chemical Shifts
    • Shen, Y.; Delaglio, F.; Cornilescu, G.; Bax, A. TALOS Plus: A Hybrid Method for Predicting Protein Torsion Angles from NMR Chemical Shifts J. Biomol. NMR 2009, 44, 213-223
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 65
    • 34547297406 scopus 로고    scopus 로고
    • Dihedral Angle Principal Component Analysis of Molecular Dynamics Simulations
    • Altis, A.; Nguyen, P. H.; Hegger, R.; Stock, G. Dihedral Angle Principal Component Analysis of Molecular Dynamics Simulations J. Chem. Phys. 2007, 126, 244111
    • (2007) J. Chem. Phys. , vol.126 , pp. 244111
    • Altis, A.1    Nguyen, P.H.2    Hegger, R.3    Stock, G.4
  • 66
    • 0020997912 scopus 로고
    • Dictionary of Protein Secondary Structure: Pattern Recognition of Hydrogen Bonded and Geometrical Features
    • Kabsch, W.; Sander, C. Dictionary of Protein Secondary Structure: Pattern Recognition of Hydrogen Bonded and Geometrical Features Biopolymers 1983, 22, 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 67
    • 0041819710 scopus 로고    scopus 로고
    • Relative Stability of Protein Structures Determined by X-ray Crystallography or NMR Spectroscopy: A Molecular Dynamics Simulation Study
    • Fan, H.; Mark, A. E. Relative Stability of Protein Structures Determined by X-ray Crystallography or NMR Spectroscopy: A Molecular Dynamics Simulation Study Proteins 2003, 53, 111-120
    • (2003) Proteins , vol.53 , pp. 111-120
    • Fan, H.1    Mark, A.E.2
  • 69
    • 84908053063 scopus 로고    scopus 로고
    • Effect of Viscogens on the Kinetic Response of a Photoperturbed Allosteric Protein
    • Waldauer, S. A.; Stucki-Buchli, B.; Frey, L.; Hamm, P. Effect of Viscogens on the Kinetic Response of a Photoperturbed Allosteric Protein J. Chem. Phys. 2014, 141, 22D514
    • (2014) J. Chem. Phys. , vol.141 , pp. 22D514
    • Waldauer, S.A.1    Stucki-Buchli, B.2    Frey, L.3    Hamm, P.4
  • 70
    • 0029881007 scopus 로고    scopus 로고
    • Molmol: A Program for Display and Analysis of Macromolecular Structures
    • Koradi, R.; Billeter, M.; Wüthrich, K. Molmol: A Program for Display and Analysis of Macromolecular Structures J. Mol. Graphics 1996, 14, 51-55
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.