메뉴 건너뛰기




Volumn 422, Issue 5, 2012, Pages 674-684

Electrostatically accelerated coupled binding and folding of intrinsically disordered proteins

Author keywords

binding kinetics; cell cycle; coarse grained modeling; induced folding; nonspecific interactions

Indexed keywords

CYCLIN A; PROTEIN P27;

EID: 84865689638     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.06.019     Document Type: Article
Times cited : (68)

References (66)
  • 1
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • P.E. Wright, and H.J. Dyson Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm J. Mol. Biol. 293 1999 321 331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 2
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev., Mol. Cell Biol. 6 2005 197 208
    • (2005) Nat. Rev., Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 5
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • P. Tompa Intrinsically unstructured proteins Trends Biochem. Sci. 27 2002 527 533
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 7
    • 78650988465 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in a physics-based world
    • T.H. Click, D. Ganguly, and J.H. Chen Intrinsically disordered proteins in a physics-based world Int. J. Mol. Sci. 11 2010 5293 5309
    • (2010) Int. J. Mol. Sci. , vol.11 , pp. 5293-5309
    • Click, T.H.1    Ganguly, D.2    Chen, J.H.3
  • 8
    • 4744349987 scopus 로고    scopus 로고
    • Combining prediction, computation and experiment for the characterization of protein disorder
    • C. Bracken, L.M. Iakoucheva, P.R. Rorner, and A.K. Dunker Combining prediction, computation and experiment for the characterization of protein disorder Curr. Opin. Struct. Biol. 14 2004 570 576
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 570-576
    • Bracken, C.1    Iakoucheva, L.M.2    Rorner, P.R.3    Dunker, A.K.4
  • 9
    • 60349087841 scopus 로고    scopus 로고
    • Biophysical characterization of intrinsically disordered proteins
    • D. Eliezer Biophysical characterization of intrinsically disordered proteins Curr. Opin. Struct. Biol. 19 2009 23 30
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 23-30
    • Eliezer, D.1
  • 10
    • 79958037883 scopus 로고    scopus 로고
    • Constructing ensembles for intrinsically disordered proteins
    • C.K. Fisher, and C.M. Stultz Constructing ensembles for intrinsically disordered proteins Curr. Opin. Struct. Biol. 21 2011 426 431
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 426-431
    • Fisher, C.K.1    Stultz, C.M.2
  • 11
    • 0035451185 scopus 로고    scopus 로고
    • Structured disorder and conformational selection
    • C.J. Tsai, B. Ma, Y.Y. Sham, S. Kumar, and R. Nussinov Structured disorder and conformational selection Proteins 44 2001 418 427
    • (2001) Proteins , vol.44 , pp. 418-427
    • Tsai, C.J.1    Ma, B.2    Sham, Y.Y.3    Kumar, S.4    Nussinov, R.5
  • 12
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • P. Tompa, C. Szasz, and L. Buday Structural disorder throws new light on moonlighting Trends Biochem. Sci. 30 2005 484 489
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3
  • 13
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • D.D. Boehr, R. Nussinov, and P.E. Wright The role of dynamic conformational ensembles in biomolecular recognition Nat. Chem. Biol. 5 2009 789 796
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 14
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • V.J. Hilser, and E.B. Thompson Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins Proc. Natl Acad. Sci. USA 104 2007 8311 8315
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 15
    • 84856708599 scopus 로고    scopus 로고
    • Intrinsic disorder: Signaling via highly specific but short-lived association
    • H.X. Zhou Intrinsic disorder: signaling via highly specific but short-lived association Trends Biochem. Sci. 37 2012 43 48
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 43-48
    • Zhou, H.X.1
  • 16
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • B.A. Shoemaker, J.J. Portman, and P.G. Wolynes Speeding molecular recognition by using the folding funnel: the fly-casting mechanism Proc. Natl Acad. Sci. USA 97 2000 8868 8873
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 17
    • 70350012289 scopus 로고    scopus 로고
    • Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: A critical assessment of the fly-casting mechanism
    • Y. Huang, and Z. Liu Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: a critical assessment of the fly-casting mechanism J. Mol. Biol. 393 2009 1143 1159
    • (2009) J. Mol. Biol. , vol.393 , pp. 1143-1159
    • Huang, Y.1    Liu, Z.2
  • 18
    • 82955239904 scopus 로고    scopus 로고
    • Automated prediction of protein association rate constants
    • S. Qin, X. Pang, and H.X. Zhou Automated prediction of protein association rate constants Structure 19 2011 1744 1751
    • (2011) Structure , vol.19 , pp. 1744-1751
    • Qin, S.1    Pang, X.2    Zhou, H.X.3
  • 19
    • 82655179928 scopus 로고    scopus 로고
    • Synergistic folding of two intrinsically disordered proteins: Searching for conformational selection
    • D. Ganguly, W. Zhang, and J. Chen Synergistic folding of two intrinsically disordered proteins: searching for conformational selection Mol. BioSyst. 8 2012 198 209
    • (2012) Mol. BioSyst. , vol.8 , pp. 198-209
    • Ganguly, D.1    Zhang, W.2    Chen, J.3
  • 20
    • 84857492391 scopus 로고    scopus 로고
    • Residual structures, conformational fluctuations, and electrostatic interactions in the synergistic folding of two intrinsically disordered proteins
    • W. Zhang, D. Ganguly, and J. Chen Residual structures, conformational fluctuations, and electrostatic interactions in the synergistic folding of two intrinsically disordered proteins PLoS Comput. Biol. 8 2012 e1002353
    • (2012) PLoS Comput. Biol. , vol.8 , pp. 1002353
    • Zhang, W.1    Ganguly, D.2    Chen, J.3
  • 21
    • 77949587817 scopus 로고    scopus 로고
    • From induced fit to conformational selection: A continuum of binding mechanism controlled by the timescale of conformational transitions
    • H.X. Zhou From induced fit to conformational selection: a continuum of binding mechanism controlled by the timescale of conformational transitions Biophys. J. 98 2010 L15 L17
    • (2010) Biophys. J. , vol.98
    • Zhou, H.X.1
  • 25
    • 47649102449 scopus 로고    scopus 로고
    • Regulation of cell division by intrinsically unstructured proteins: Intrinsic flexibility, modularity, and signaling conduits
    • C.A. Galea, Y. Wang, S.G. Sivakolundu, and R.W. Kriwacki Regulation of cell division by intrinsically unstructured proteins: intrinsic flexibility, modularity, and signaling conduits Biochemistry 47 2008 7598 7609
    • (2008) Biochemistry , vol.47 , pp. 7598-7609
    • Galea, C.A.1    Wang, Y.2    Sivakolundu, S.G.3    Kriwacki, R.W.4
  • 26
    • 38849187293 scopus 로고    scopus 로고
    • CDK inhibitors: Cell cycle regulators and beyond
    • A. Besson, S.F. Dowdy, and J.M. Roberts CDK inhibitors: cell cycle regulators and beyond Dev. Cell 14 2008 159 169
    • (2008) Dev. Cell , vol.14 , pp. 159-169
    • Besson, A.1    Dowdy, S.F.2    Roberts, J.M.3
  • 28
    • 0032096837 scopus 로고    scopus 로고
    • Continuum solvation model: Electrostatic forces from numerical solutions to the Poisson-Boltzmann equation
    • W. Im, D. Beglov, and B. Roux Continuum solvation model: electrostatic forces from numerical solutions to the Poisson-Boltzmann equation Comput. Phys. Commun. 111 1998 59 75
    • (1998) Comput. Phys. Commun. , vol.111 , pp. 59-75
    • Im, W.1    Beglov, D.2    Roux, B.3
  • 29
    • 27144528728 scopus 로고    scopus 로고
    • Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation
    • Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation J. Mol. Biol. 353 2005 1118 1128
    • (2005) J. Mol. Biol. , vol.353 , pp. 1118-1128
    • Sivakolundu, S.G.1    Bashford, D.2    Kriwacki, R.W.3
  • 30
    • 79952959945 scopus 로고    scopus 로고
    • Intrinsic disorder mediates the diverse regulatory functions of the Cdk inhibitor p21
    • Y.F. Wang, J.C. Fisher, R. Mathew, L. Ou, S. Otieno, and J. Sublet Intrinsic disorder mediates the diverse regulatory functions of the Cdk inhibitor p21 Nat. Chem. Biol. 7 2011 214 221
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 214-221
    • Wang, Y.F.1    Fisher, J.C.2    Mathew, R.3    Ou, L.4    Otieno, S.5    Sublet, J.6
  • 31
    • 1842473094 scopus 로고    scopus 로고
    • P27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding
    • E.R. Lacy, I. Filippov, W.S. Lewis, S. Otieno, L.M. Xiao, and S. Weiss p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding Nat. Struct. Mol. Biol. 11 2004 358 364
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 358-364
    • Lacy, E.R.1    Filippov, I.2    Lewis, W.S.3    Otieno, S.4    Xiao, L.M.5    Weiss, S.6
  • 32
    • 79959639498 scopus 로고    scopus 로고
    • The role of the LH subdomain in the function of the Cip/Kip cyclin-dependent kinase regulators
    • S. Otieno, C.R. Grace, and R.W. Kriwacki The role of the LH subdomain in the function of the Cip/Kip cyclin-dependent kinase regulators Biophys. J. 100 2011 2486 2494
    • (2011) Biophys. J. , vol.100 , pp. 2486-2494
    • Otieno, S.1    Grace, C.R.2    Kriwacki, R.W.3
  • 34
    • 0037627721 scopus 로고    scopus 로고
    • Simulating disorder-order transitions in molecular recognition of unstructured proteins: Where folding meets binding
    • G.M. Verkhivker, D. Bouzida, D.K. Gehlhaar, P.A. Rejto, S.T. Freer, and P.W. Rose Simulating disorder-order transitions in molecular recognition of unstructured proteins: where folding meets binding Proc. Natl Acad. Sci. USA 100 2003 5148 5153
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5148-5153
    • Verkhivker, G.M.1    Bouzida, D.2    Gehlhaar, D.K.3    Rejto, P.A.4    Freer, S.T.5    Rose, P.W.6
  • 35
    • 65249099497 scopus 로고    scopus 로고
    • Fundamental aspects of protein-protein association kinetics
    • G. Schreiber, G. Haran, and H.X. Zhou Fundamental aspects of protein-protein association kinetics Chem. Rev. 109 2009 839 860
    • (2009) Chem. Rev. , vol.109 , pp. 839-860
    • Schreiber, G.1    Haran, G.2    Zhou, H.X.3
  • 36
    • 66149107139 scopus 로고    scopus 로고
    • Simulating the electrostatic guidance of the vectorial translocations in hexameric helicases and translocases
    • H. Liu, Y. Shi, X.S. Chen, and A. Warshel Simulating the electrostatic guidance of the vectorial translocations in hexameric helicases and translocases Proc. Natl Acad. Sci. USA 106 2009 7449 7454
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 7449-7454
    • Liu, H.1    Shi, Y.2    Chen, X.S.3    Warshel, A.4
  • 37
    • 81055141525 scopus 로고    scopus 로고
    • Frustration in protein-DNA binding influences conformational switching and target search kinetics
    • A. Marcovitz, and Y. Levy Frustration in protein-DNA binding influences conformational switching and target search kinetics Proc. Natl Acad. Sci. USA 108 2011 17957 17962
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 17957-17962
    • Marcovitz, A.1    Levy, Y.2
  • 38
    • 70349422120 scopus 로고    scopus 로고
    • Nonnative electrostatic interactions can modulate protein folding: Molecular dynamics with a grain of salt
    • A. Azia, and Y. Levy Nonnative electrostatic interactions can modulate protein folding: molecular dynamics with a grain of salt J. Mol. Biol. 393 2009 527 542
    • (2009) J. Mol. Biol. , vol.393 , pp. 527-542
    • Azia, A.1    Levy, Y.2
  • 39
    • 0141990950 scopus 로고    scopus 로고
    • Effect of gatekeepers on the early folding kinetics of a model β-barrel protein
    • A.D. Stoycheva, J.N. Onuchic, and C.L. Brooks Effect of gatekeepers on the early folding kinetics of a model β-barrel protein J. Chem. Phys. 119 2003 5722 5729
    • (2003) J. Chem. Phys. , vol.119 , pp. 5722-5729
    • Stoycheva, A.D.1    Onuchic, J.N.2    Brooks, C.L.3
  • 40
    • 2942705984 scopus 로고    scopus 로고
    • Gatekeepers in the ribosomal protein S6: Thermodynamics, kinetics, and folding pathways revealed by a minimalist protein model
    • A.D. Stoycheva, C.L. Brooks, and J.N. Onuchic Gatekeepers in the ribosomal protein S6: thermodynamics, kinetics, and folding pathways revealed by a minimalist protein model J. Mol. Biol. 340 2004 571 585
    • (2004) J. Mol. Biol. , vol.340 , pp. 571-585
    • Stoycheva, A.D.1    Brooks, C.L.2    Onuchic, J.N.3
  • 41
    • 0032718386 scopus 로고    scopus 로고
    • Salt-induced detour through compact regions of the protein folding landscape
    • D.E. Otzen, and M. Oliveberg Salt-induced detour through compact regions of the protein folding landscape Proc. Natl Acad. Sci. USA 96 1999 11746 11751
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11746-11751
    • Otzen, D.E.1    Oliveberg, M.2
  • 42
    • 77952335311 scopus 로고    scopus 로고
    • Net charge per residue modulates conformational ensembles of intrinsically disordered proteins
    • A.H. Mao, S.L. Crick, A. Vitalis, C.L. Chicoine, and R.V. Pappu Net charge per residue modulates conformational ensembles of intrinsically disordered proteins Proc. Natl Acad. Sci. USA 107 2010 8183 8188
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 8183-8188
    • Mao, A.H.1    Crick, S.L.2    Vitalis, A.3    Chicoine, C.L.4    Pappu, R.V.5
  • 44
    • 79952489792 scopus 로고    scopus 로고
    • Topology-based modeling of intrinsically disordered proteins: Balancing intrinsic folding and intermolecular interactions
    • D. Ganguly, and J. Chen Topology-based modeling of intrinsically disordered proteins: balancing intrinsic folding and intermolecular interactions Proteins: Struct., Funct., Bioinf. 79 2011 1251 1266
    • (2011) Proteins: Struct., Funct., Bioinf. , vol.79 , pp. 1251-1266
    • Ganguly, D.1    Chen, J.2
  • 45
    • 78149492409 scopus 로고    scopus 로고
    • Nonnative interactions in coupled folding and binding processes of intrinsically disordered proteins
    • Y. Huang, and Z. Liu Nonnative interactions in coupled folding and binding processes of intrinsically disordered proteins PLoS One 5 2010 e15375
    • (2010) PLoS One , vol.5 , pp. 15375
    • Huang, Y.1    Liu, Z.2
  • 46
    • 82655179907 scopus 로고    scopus 로고
    • Modulation of an IDP binding mechanism and rates by helix propensity and non-native interactions: Association of HIF1α with CBP
    • D. De Sancho, and R.B. Best Modulation of an IDP binding mechanism and rates by helix propensity and non-native interactions: association of HIF1α with CBP Mol. BioSyst. 8 2012 256 267
    • (2012) Mol. BioSyst. , vol.8 , pp. 256-267
    • De Sancho, D.1    Best, R.B.2
  • 47
    • 33846625611 scopus 로고    scopus 로고
    • Fly-casting in protein-DNA binding: Frustration between protein folding and electrostatics facilitates target recognition
    • Y. Levy, J.N. Onuchic, and P.G. Wolynes Fly-casting in protein-DNA binding: frustration between protein folding and electrostatics facilitates target recognition J. Am. Chem. Soc. 129 2007 738 739
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 738-739
    • Levy, Y.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 48
    • 0034669882 scopus 로고    scopus 로고
    • Why are natively unfolded proteins unstructured under physiologic conditions?
    • V.N. Uversky, J.R. Gillespie, and A.L. Fink Why are natively unfolded proteins unstructured under physiologic conditions? Proteins 41 2000 415 427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 49
    • 34547943482 scopus 로고    scopus 로고
    • Molecular principles of the interactions of disordered proteins
    • B. Meszaros, P. Tompa, I. Simon, and Z. Dosztanyi Molecular principles of the interactions of disordered proteins J. Mol. Biol. 372 2007 549 561
    • (2007) J. Mol. Biol. , vol.372 , pp. 549-561
    • Meszaros, B.1    Tompa, P.2    Simon, I.3    Dosztanyi, Z.4
  • 50
    • 67949106402 scopus 로고    scopus 로고
    • Intrinsically disordered p53 extreme C-terminus binds to S100B(ββ) through fly-casting
    • J.H. Chen Intrinsically disordered p53 extreme C-terminus binds to S100B(ββ) through fly-casting J. Am. Chem. Soc. 131 2009 2088 2089
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2088-2089
    • Chen, J.H.1
  • 51
    • 50249134423 scopus 로고    scopus 로고
    • Kinetics of folding and binding of an intrinsically disordered protein: The inhibitor of yeast aspartic proteinase YPrA
    • R. Narayanan, O.K. Ganesh, A.S. Edison, and S.J. Hagen Kinetics of folding and binding of an intrinsically disordered protein: the inhibitor of yeast aspartic proteinase YPrA J. Am. Chem. Soc. 130 2008 11477 11485
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11477-11485
    • Narayanan, R.1    Ganesh, O.K.2    Edison, A.S.3    Hagen, S.J.4
  • 53
    • 42949161558 scopus 로고    scopus 로고
    • Binding-induced folding of a natively unstructured transcription factor
    • A.G. Turjanski, J.S. Gutkind, R.B. Best, and G. Hummer Binding-induced folding of a natively unstructured transcription factor PLoS Comput. Biol. 4 2008 e1000060
    • (2008) PLoS Comput. Biol. , vol.4 , pp. 1000060
    • Turjanski, A.G.1    Gutkind, J.S.2    Best, R.B.3    Hummer, G.4
  • 54
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • K. Sugase, H.J. Dyson, and P.E. Wright Mechanism of coupled folding and binding of an intrinsically disordered protein Nature 447 2007 1021 1025
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 55
    • 79952741171 scopus 로고    scopus 로고
    • Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction
    • A. Bachmann, D. Wildemann, F. Praetorius, G. Fischer, and T. Kiefhaber Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction Proc. Natl Acad. Sci. USA 108 2011 3952 3957
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 3952-3957
    • Bachmann, A.1    Wildemann, D.2    Praetorius, F.3    Fischer, G.4    Kiefhaber, T.5
  • 56
    • 33947586778 scopus 로고    scopus 로고
    • Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics
    • Q. Lu, H.P. Lu, and J. Wang Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics Phys. Rev. Lett. 98 2007 128105
    • (2007) Phys. Rev. Lett. , vol.98 , pp. 128105
    • Lu, Q.1    Lu, H.P.2    Wang, J.3
  • 57
    • 77649264931 scopus 로고    scopus 로고
    • Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins
    • Z. Zhang, and H.S. Chan Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins Proc. Natl Acad. Sci. USA 107 2010 2920 2925
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 2920-2925
    • Zhang, Z.1    Chan, H.S.2
  • 58
    • 70350321301 scopus 로고    scopus 로고
    • Disordered tails of homeodomains facilitate DNA recognition by providing a trade-off between folding and specific binding
    • A.g. ToÍth-PetroÍczy, I. Simon, M. Fuxreiter, and Y. Levy Disordered tails of homeodomains facilitate DNA recognition by providing a trade-off between folding and specific binding J. Am. Chem. Soc. 131 2009 15084 15085
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15084-15085
    • ToÍth-PetroÍczy, A.G.1    Simon, I.2    Fuxreiter, M.3    Levy, Y.4
  • 59
    • 33846268807 scopus 로고    scopus 로고
    • P27 phosphorylation by Src regulates inhibition of cyclin E-Cdk2
    • I. Chu, J. Sun, A. Arnaout, H. Kahn, W. Hanna, and S. Narod p27 phosphorylation by Src regulates inhibition of cyclin E-Cdk2 Cell 128 2007 281 294
    • (2007) Cell , vol.128 , pp. 281-294
    • Chu, I.1    Sun, J.2    Arnaout, A.3    Kahn, H.4    Hanna, W.5    Narod, S.6
  • 61
    • 0036785556 scopus 로고    scopus 로고
    • The origins of asymmetry in the folding transition states of protein L and protein G
    • J. Karanicolas, and C.L. Brooks The origins of asymmetry in the folding transition states of protein L and protein G Protein Sci. 11 2002 2351 2361
    • (2002) Protein Sci. , vol.11 , pp. 2351-2361
    • Karanicolas, J.1    Brooks, C.L.2
  • 64
    • 1942423619 scopus 로고    scopus 로고
    • MMTSB Tool Set: Enhanced sampling and multiscale modeling methods for applications in structural biology
    • M. Feig, J. Karanicolas, and C.L. Brooks MMTSB Tool Set: enhanced sampling and multiscale modeling methods for applications in structural biology J. Mol. Graphics Modell. 22 2004 377 395
    • (2004) J. Mol. Graphics Modell. , vol.22 , pp. 377-395
    • Feig, M.1    Karanicolas, J.2    Brooks, C.L.3
  • 65
    • 17444366185 scopus 로고    scopus 로고
    • Temperature weighted histogram analysis method, replica exchange, and transition paths
    • E. Gallicchio, M. Andrec, A.K. Felts, and R.M. Levy Temperature weighted histogram analysis method, replica exchange, and transition paths J. Phys. Chem. B 109 2005 6722 6731
    • (2005) J. Phys. Chem. B , vol.109 , pp. 6722-6731
    • Gallicchio, E.1    Andrec, M.2    Felts, A.K.3    Levy, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.