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Volumn 7, Issue 8, 2011, Pages

Binding free energy landscape of domain-peptide interactions

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; C (PROGRAMMING LANGUAGE); ENERGY BARRIERS; FREE ENERGY; TEMPERATURE DISTRIBUTION;

EID: 80052312953     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1002131     Document Type: Article
Times cited : (21)

References (64)
  • 1
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE, (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6: 197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 3
    • 49549083915 scopus 로고    scopus 로고
    • Peptide-mediated interactions in biological systems: new discoveries and applications
    • Petsalaki E, Russell RB, (2008) Peptide-mediated interactions in biological systems: new discoveries and applications. Curr Opin Biotechnol 19: 344-350.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 344-350
    • Petsalaki, E.1    Russell, R.B.2
  • 4
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson T, Nash P, (2003) Assembly of cell regulatory systems through protein interaction domains. Science 300: 445-452.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 5
    • 33746363486 scopus 로고    scopus 로고
    • Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits
    • Bhattacharyya RP, Remenyi A, Yeh BJ, Lim WA, (2006) Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. Annu Rev Biochem 75: 655-680.
    • (2006) Annu Rev Biochem , vol.75 , pp. 655-680
    • Bhattacharyya, R.P.1    Remenyi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 6
    • 54249117223 scopus 로고    scopus 로고
    • Targeting and tinkering with interaction networks
    • Russell RB, Aloy P, (2008) Targeting and tinkering with interaction networks. Nat Chem Biol 4: 666-673.
    • (2008) Nat Chem Biol , vol.4 , pp. 666-673
    • Russell, R.B.1    Aloy, P.2
  • 7
    • 64849111005 scopus 로고    scopus 로고
    • Sending signals dynamically
    • Smock RG, Gierasch LM, (2009) Sending signals dynamically. Science 324: 198-203.
    • (2009) Science , vol.324 , pp. 198-203
    • Smock, R.G.1    Gierasch, L.M.2
  • 8
    • 33748953868 scopus 로고    scopus 로고
    • Peptides mediating interaction networks: new leads at last
    • Neduva V, Russell RB, (2006) Peptides mediating interaction networks: new leads at last. Curr Opin Biotechnol 17: 465-471.
    • (2006) Curr Opin Biotechnol , vol.17 , pp. 465-471
    • Neduva, V.1    Russell, R.B.2
  • 9
    • 67349275522 scopus 로고    scopus 로고
    • Peptidic modulators of protein-protein interactions: progress and challenges in computational design
    • Rubinstein M, Niv MY, (2009) Peptidic modulators of protein-protein interactions: progress and challenges in computational design. Biopolymers 91: 505-513.
    • (2009) Biopolymers , vol.91 , pp. 505-513
    • Rubinstein, M.1    Niv, M.Y.2
  • 10
    • 0031020376 scopus 로고    scopus 로고
    • Computation of the binding of fully flexible peptides to proteins with flexible side chains
    • Desmet J, Wilson IA, Joniau M, De Maeyer M, Lasters I, (1997) Computation of the binding of fully flexible peptides to proteins with flexible side chains. FASEB J 11: 164-172.
    • (1997) FASEB J , vol.11 , pp. 164-172
    • Desmet, J.1    Wilson, I.A.2    Joniau, M.3    De Maeyer, M.4    Lasters, I.5
  • 11
    • 3142745414 scopus 로고    scopus 로고
    • Structural mining: self-consistent design on flexible protein-peptide docking and transferable binding affinity potential
    • Liu Z, Dominy BN, Shakhnovich EI, (2004) Structural mining: self-consistent design on flexible protein-peptide docking and transferable binding affinity potential. J Am Chem Soc 126: 8515-8528.
    • (2004) J Am Chem Soc , vol.126 , pp. 8515-8528
    • Liu, Z.1    Dominy, B.N.2    Shakhnovich, E.I.3
  • 12
    • 4344589929 scopus 로고    scopus 로고
    • Modeling the structure of bound peptide ligands to major histocompatibility complex
    • Tong JC, Tan TW, Ranganathan S, (2004) Modeling the structure of bound peptide ligands to major histocompatibility complex. Protein Sci 13: 2523-2532.
    • (2004) Protein Sci , vol.13 , pp. 2523-2532
    • Tong, J.C.1    Tan, T.W.2    Ranganathan, S.3
  • 13
    • 26444604826 scopus 로고    scopus 로고
    • A flexible docking procedure for the exploration of peptide binding selectivity to known structures and homology models of PDZ domains
    • Niv MY, Weinstein H, (2005) A flexible docking procedure for the exploration of peptide binding selectivity to known structures and homology models of PDZ domains. J Am Chem Soc 127: 14072-14079.
    • (2005) J Am Chem Soc , vol.127 , pp. 14072-14079
    • Niv, M.Y.1    Weinstein, H.2
  • 14
    • 77953573815 scopus 로고    scopus 로고
    • Sub-angstrom modeling of complexes between flexible peptides and globular proteins
    • Raveh B, London N, Schueler-Furman O, (2010) Sub-angstrom modeling of complexes between flexible peptides and globular proteins. Proteins 78: 2029-2040.
    • (2010) Proteins , vol.78 , pp. 2029-2040
    • Raveh, B.1    London, N.2    Schueler-Furman, O.3
  • 15
    • 78349258533 scopus 로고    scopus 로고
    • Structure-based prediction of protein-peptide specificity in Rosetta
    • King CA, Bradley P, (2010) Structure-based prediction of protein-peptide specificity in Rosetta. Proteins 78: 3437-3449.
    • (2010) Proteins , vol.78 , pp. 3437-3449
    • King, C.A.1    Bradley, P.2
  • 16
    • 79551585392 scopus 로고    scopus 로고
    • A physical model for PDZdomain/peptide interactions
    • Kaufmann K, Shen N, Mizoue L, Meiler J, (2011) A physical model for PDZdomain/peptide interactions. J Mol Model 17: 315-324.
    • (2011) J Mol Model , vol.17 , pp. 315-324
    • Kaufmann, K.1    Shen, N.2    Mizoue, L.3    Meiler, J.4
  • 17
    • 0036084259 scopus 로고    scopus 로고
    • Efficient docking of peptides to proteins without prior knowledge of the binding site
    • Hetnyi C, van der Spoel D, (2002) Efficient docking of peptides to proteins without prior knowledge of the binding site. Protein Sci 11: 1729-1737.
    • (2002) Protein Sci , vol.11 , pp. 1729-1737
    • Hetnyi, C.1    van der Spoel, D.2
  • 19
    • 69049083531 scopus 로고    scopus 로고
    • Using genome-wide measurements for computational prediction of SH2-peptide interactions
    • Wunderlich Z, Mirny LA, (2009) Using genome-wide measurements for computational prediction of SH2-peptide interactions. Nucleic Acids Res 37: 4629-4641.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4629-4641
    • Wunderlich, Z.1    Mirny, L.A.2
  • 20
    • 67349248904 scopus 로고    scopus 로고
    • Structure-based prediction of the Saccharomyces cerevisiae SH3-ligand interactions
    • Fernandez-Ballester G, Beltrao P, Gonzalez JM, Song YH, Wilmanns M, et al. (2009) Structure-based prediction of the Saccharomyces cerevisiae SH3-ligand interactions. J Mol Biol 388: 902-916.
    • (2009) J Mol Biol , vol.388 , pp. 902-916
    • Fernandez-Ballester, G.1    Beltrao, P.2    Gonzalez, J.M.3    Song, Y.H.4    Wilmanns, M.5
  • 21
    • 66149146342 scopus 로고    scopus 로고
    • Characterization of domain-peptide interaction interface: a generic structure-based model to decipher the binding specificity of SH3 domains
    • Hou T, Xu Z, Zhang W, McLaughlin WA, Case DA, et al. (2009) Characterization of domain-peptide interaction interface: a generic structure-based model to decipher the binding specificity of SH3 domains. Mol Cell Proteomics 8: 639-649.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 639-649
    • Hou, T.1    Xu, Z.2    Zhang, W.3    McLaughlin, W.A.4    Case, D.A.5
  • 23
    • 5044232231 scopus 로고    scopus 로고
    • Conformational flexibility of the MHC class I alpha1-alpha2 domain in peptide bound and free states: a molecular dynamics simulation study
    • Zacharias M, Springer S, (2004) Conformational flexibility of the MHC class I alpha1-alpha2 domain in peptide bound and free states: a molecular dynamics simulation study. Biophys J 87: 2203-2214.
    • (2004) Biophys J , vol.87 , pp. 2203-2214
    • Zacharias, M.1    Springer, S.2
  • 24
    • 33749511033 scopus 로고    scopus 로고
    • Thermodynamic basis for promiscuity and selectivity in protein-protein interactions: PDZ domains, a case study
    • Basdevant N, Weinstein H, Ceruso M, (2006) Thermodynamic basis for promiscuity and selectivity in protein-protein interactions: PDZ domains, a case study. J Am Chem Soc 128: 12766-12777.
    • (2006) J Am Chem Soc , vol.128 , pp. 12766-12777
    • Basdevant, N.1    Weinstein, H.2    Ceruso, M.3
  • 25
    • 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, (2008) Mapping of two networks of residues that exhibit structural and dynamical changes upon binding in a PDZ domain protein. J Am Chem Soc 130: 8931-8939.
    • (2008) J Am Chem Soc , vol.130 , pp. 8931-8939
    • Dhulesia, A.1    Gsponer, J.2    Vendruscolo, M.3
  • 26
    • 70350010160 scopus 로고    scopus 로고
    • All-atom Monte Carlo approach to protein-peptide binding
    • Staneva I, Wallin S, (2009) All-atom Monte Carlo approach to protein-peptide binding. J Mol Biol 393: 1118-1128.
    • (2009) J Mol Biol , vol.393 , pp. 1118-1128
    • Staneva, I.1    Wallin, S.2
  • 27
    • 0041629626 scopus 로고    scopus 로고
    • Thermodynamics of alphaand beta-structure formation in proteins
    • Irbäck A, Samuelsson B, Sjunnesson F, Wallin S, (2003) Thermodynamics of alphaand beta-structure formation in proteins. Biophys J 85: 1466-1473.
    • (2003) Biophys J , vol.85 , pp. 1466-1473
    • Irbäck, A.1    Samuelsson, B.2    Sjunnesson, F.3    Wallin, S.4
  • 28
    • 33748604047 scopus 로고    scopus 로고
    • PROFASI: A Monte Carlo simulation package for protein folding and aggregation
    • Irbäck A, Mohanty S, (2006) PROFASI: A Monte Carlo simulation package for protein folding and aggregation. J Comput Chem 27: 1548-1555.
    • (2006) J Comput Chem , vol.27 , pp. 1548-1555
    • Irbäck, A.1    Mohanty, S.2
  • 30
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M, Sala C, (2001) PDZ domains and the organization of supramolecular complexes. Annu Rev Neurosci 24: 1-29.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 31
    • 39049128059 scopus 로고    scopus 로고
    • Act globally, think locally: systems biology addresses the PDZ domain
    • Spaller MR, (2006) Act globally, think locally: systems biology addresses the PDZ domain. ACS Chem Biol 1: 207-210.
    • (2006) ACS Chem Biol , vol.1 , pp. 207-210
    • Spaller, M.R.1
  • 32
    • 77952705907 scopus 로고    scopus 로고
    • PDZ domains and their binding partners: structure, specificity, and modification
    • Lee HJ, Zheng JJ, (2010) PDZ domains and their binding partners: structure, specificity, and modification. Cell Commun Signal 8: 8.
    • (2010) Cell Commun Signal , vol.8 , pp. 8
    • Lee, H.J.1    Zheng, J.J.2
  • 36
    • 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 DA, Lee A, Lewis J, Kim E, Sheng M, et al. (1996) Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 85: 1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5
  • 37
    • 0037424515 scopus 로고    scopus 로고
    • Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization
    • Im YJ, Park SH, Rho SH, Lee JH, Kang GB, et al. (2003) Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization. J Biol Chem 278: 8501-8507.
    • (2003) J Biol Chem , vol.278 , pp. 8501-8507
    • Im, Y.J.1    Park, S.H.2    Rho, S.H.3    Lee, J.H.4    Kang, G.B.5
  • 38
    • 34249679667 scopus 로고    scopus 로고
    • A thermodynamic ligand binding study of the third PDZ domain (PDZ3) from the mammalian neuronal protein PSD-95
    • Saro D, Li T, Rupasinghe C, Paredes A, Caspers N, et al. (2007) A thermodynamic ligand binding study of the third PDZ domain (PDZ3) from the mammalian neuronal protein PSD-95. Biochemistry 46: 6340-6352.
    • (2007) Biochemistry , vol.46 , pp. 6340-6352
    • Saro, D.1    Li, T.2    Rupasinghe, C.3    Paredes, A.4    Caspers, N.5
  • 39
    • 27144437020 scopus 로고    scopus 로고
    • The kinetics of PDZ domain-ligand interactions and implications for the binding mechanism
    • Gianni S, Engström Å, Larsson M, Calosci N, Malatesta F, et al. (2005) The kinetics of PDZ domain-ligand interactions and implications for the binding mechanism. J Biol Chem 280: 34805-34812.
    • (2005) J Biol Chem , vol.280 , pp. 34805-34812
    • Gianni, S.1    Engström, A.2    Larsson, M.3    Calosci, N.4    Malatesta, F.5
  • 41
    • 35648957794 scopus 로고    scopus 로고
    • Clustering and synaptic targeting of PICK1 requires direct interaction between the PDZ domain and lipid membranes
    • Pan L, Wu H, Shen C, Shi Y, Jin W, et al. (2007) Clustering and synaptic targeting of PICK1 requires direct interaction between the PDZ domain and lipid membranes. EMBO J 26: 4576-4587.
    • (2007) EMBO J , vol.26 , pp. 4576-4587
    • Pan, L.1    Wu, H.2    Shen, C.3    Shi, Y.4    Jin, W.5
  • 42
    • 33947712970 scopus 로고    scopus 로고
    • Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions
    • Elkins JM, Papagrigoriou E, Berridge G, Yang X, Phillips C, et al. (2007) Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions. Protein Sci 16: 683-694.
    • (2007) Protein Sci , vol.16 , pp. 683-694
    • Elkins, J.M.1    Papagrigoriou, E.2    Berridge, G.3    Yang, X.4    Phillips, C.5
  • 43
    • 4744341240 scopus 로고    scopus 로고
    • The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and GluR2 as interacting ligands
    • Dev KK, Nakanishi S, Henley JM, (2004) The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and GluR2 as interacting ligands. J Biol Chem 279: 41393-41397.
    • (2004) J Biol Chem , vol.279 , pp. 41393-41397
    • Dev, K.K.1    Nakanishi, S.2    Henley, J.M.3
  • 44
    • 20144374482 scopus 로고    scopus 로고
    • Molecular determinants for the complex binding specificity of the PDZ domain in PICK1
    • Madsen KL, Beuming T, Niv MY, Chang CW, Dev KK, et al. (2005) Molecular determinants for the complex binding specificity of the PDZ domain in PICK1. J Biol Chem 280: 20539-20548.
    • (2005) J Biol Chem , vol.280 , pp. 20539-20548
    • Madsen, K.L.1    Beuming, T.2    Niv, M.Y.3    Chang, C.W.4    Dev, K.K.5
  • 45
    • 33644899039 scopus 로고
    • Simulated tempering: a new Monte Carlo scheme
    • Marinari E, Parisi G, (1992) Simulated tempering: a new Monte Carlo scheme. Europhys Lett 19: 451-458.
    • (1992) Europhys Lett , vol.19 , pp. 451-458
    • Marinari, E.1    Parisi, G.2
  • 47
    • 0000773431 scopus 로고
    • Studies of an off-lattice model for protein folding: sequence dependence and improved sampling at finite temperature
    • Irbäck A, Potthast F, (1995) Studies of an off-lattice model for protein folding: sequence dependence and improved sampling at finite temperature. J Chem Phys 103: 10298-10305.
    • (1995) J Chem Phys , vol.103 , pp. 10298-10305
    • Irbäck, A.1    Potthast, F.2
  • 48
    • 70450065485 scopus 로고    scopus 로고
    • Identification of specificity and promiscuity of PDZ domain interactions through their dynamic behavior
    • Gerek ZN, Keskin O, Ozkan SB, (2009) Identification of specificity and promiscuity of PDZ domain interactions through their dynamic behavior. Proteins 77: 796-811.
    • (2009) Proteins , vol.77 , pp. 796-811
    • Gerek, Z.N.1    Keskin, O.2    Ozkan, S.B.3
  • 49
    • 58949102247 scopus 로고    scopus 로고
    • Signaling pathways of PDZ2 domain: a molecular dynamics interaction correlation analysis
    • Kong Y, Karplus M, (2009) Signaling pathways of PDZ2 domain: a molecular dynamics interaction correlation analysis. Proteins 74: 145-154.
    • (2009) Proteins , vol.74 , pp. 145-154
    • Kong, Y.1    Karplus, M.2
  • 50
    • 33947252405 scopus 로고    scopus 로고
    • Binding induced folding in p53-MDM2 complex
    • Chen H, Luo R, (2007) Binding induced folding in p53-MDM2 complex. J Am Chem Soc 129: 2930-2937.
    • (2007) J Am Chem Soc , vol.129 , pp. 2930-2937
    • Chen, H.1    Luo, R.2
  • 51
    • 67949106402 scopus 로고    scopus 로고
    • Intrinsically disordered p53 extreme C-terminus binds to S100B(ββ) through "fly-casting"
    • Chen J, (2009) Intrinsically disordered p53 extreme C-terminus binds to S100B(ββ) through "fly-casting". J Am Chem Soc 131: 2088-2089.
    • (2009) J Am Chem Soc , vol.131 , pp. 2088-2089
    • Chen, J.1
  • 52
    • 79960041673 scopus 로고    scopus 로고
    • A free-energy landscape for coupled folding and binding of an intrinsically disordered protein in explicit solvent from detailed all-atom computations
    • In Press
    • Higo J, Nishimura Y, Nakamura H, (2011) A free-energy landscape for coupled folding and binding of an intrinsically disordered protein in explicit solvent from detailed all-atom computations. J Am Chem Soc In Press.
    • (2011) J Am Chem Soc
    • Higo, J.1    Nishimura, Y.2    Nakamura, H.3
  • 53
    • 79952260271 scopus 로고    scopus 로고
    • Anchoring intrinsically disordered proteins to multiple targets: Lessons from N-terminus of the p53 protein
    • Huang Y, Liu Z, (2011) Anchoring intrinsically disordered proteins to multiple targets: Lessons from N-terminus of the p53 protein. Int J Mol Sci 12: 1410-1430.
    • (2011) Int J Mol Sci , vol.12 , pp. 1410-1430
    • Huang, Y.1    Liu, Z.2
  • 54
    • 79955570145 scopus 로고    scopus 로고
    • Multi-scaled explorations of binding-induced folding of intrinsically disordered protein inhibitor IA3 to its target enzyme
    • Wang J, Wang Y, Chu X, Hagen SJ, Han W, et al. (2011) Multi-scaled explorations of binding-induced folding of intrinsically disordered protein inhibitor IA3 to its target enzyme. PLoS Comput Biol 7: e1001118.
    • (2011) PLoS Comput Biol , vol.7
    • Wang, J.1    Wang, Y.2    Chu, X.3    Hagen, S.J.4    Han, W.5
  • 55
    • 0032756923 scopus 로고    scopus 로고
    • The 'dynamics' in the thermodynamics of binding
    • Forman-Kay JD, (1999) The 'dynamics' in the thermodynamics of binding. Nat Struct Biol 6: 1086-1087.
    • (1999) Nat Struct Biol , vol.6 , pp. 1086-1087
    • Forman-Kay, J.D.1
  • 56
    • 33846822002 scopus 로고    scopus 로고
    • Ligand configurational entropy and protein binding
    • Chang CE, Chen W, Gilson MK, (2007) Ligand configurational entropy and protein binding. Proc Natl Acad Sci USA 104: 1534-1539.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1534-1539
    • Chang, C.E.1    Chen, W.2    Gilson, M.K.3
  • 57
    • 65549109031 scopus 로고    scopus 로고
    • Configurational entropy in protein-peptide binding: computational study of Tsg101 ubiquitin E2 variant domain with an HIV-derived PTAP nonapeptide
    • Killian BJ, Kravitz JY, Somani S, Dasgupta P, Pang YP, et al. (2009) Configurational entropy in protein-peptide binding: computational study of Tsg101 ubiquitin E2 variant domain with an HIV-derived PTAP nonapeptide. J Mol Biol 389: 315-335.
    • (2009) J Mol Biol , vol.389 , pp. 315-335
    • Killian, B.J.1    Kravitz, J.Y.2    Somani, S.3    Dasgupta, P.4    Pang, Y.P.5
  • 58
    • 13444301037 scopus 로고    scopus 로고
    • A survey of flexible protein binding mechanisms and their transition states using native topology based energy landscapes
    • Levy Y, Cho SS, Onuchic JN, Wolynes PG, (2005) A survey of flexible protein binding mechanisms and their transition states using native topology based energy landscapes. J Mol Biol 346: 1121-1145.
    • (2005) J Mol Biol , vol.346 , pp. 1121-1145
    • Levy, Y.1    Cho, S.S.2    Onuchic, J.N.3    Wolynes, P.G.4
  • 59
    • 70350012289 scopus 로고    scopus 로고
    • Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: a critical assessment of the "fly-casting" mechanism
    • Huang Y, Liu Z, (2009) Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: a critical assessment of the "fly-casting" mechanism. J Mol Biol 393: 1143-1159.
    • (2009) J Mol Biol , vol.393 , pp. 1143-1159
    • Huang, Y.1    Liu, Z.2
  • 60
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai CJ, Kumar S, Ma B, Nussinov R, (1999) Folding funnels, binding funnels, and protein function. Protein Sci 8: 1181-1190.
    • (1999) Protein Sci , vol.8 , pp. 1181-1190
    • Tsai, C.J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 61
    • 77950261885 scopus 로고    scopus 로고
    • Unusual binding interactions in PDZ domain crystal structures help explain binding mechanisms
    • Elkins JM, Gileadi C, Shrestha L, Phillips C, Wang J, et al. (2010) Unusual binding interactions in PDZ domain crystal structures help explain binding mechanisms. Protein Sci 19: 731-741.
    • (2010) Protein Sci , vol.19 , pp. 731-741
    • Elkins, J.M.1    Gileadi, C.2    Shrestha, L.3    Phillips, C.4    Wang, J.5
  • 62
    • 26944496474 scopus 로고    scopus 로고
    • Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem
    • Long JF, Feng W, Wang R, Chan LN, Ip FCF, et al. (2005) Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem. Nat Struct Mol Biol 12: 722-728.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 722-728
    • Long, J.F.1    Feng, W.2    Wang, R.3    Chan, L.N.4    Ip, F.C.F.5
  • 63
    • 0035826575 scopus 로고    scopus 로고
    • Monte Carlo update for chain molecules: biased Gaussian steps in torsional space
    • Favrin G, Irbäck A, Sjunnesson F, (2001) Monte Carlo update for chain molecules: biased Gaussian steps in torsional space. J Chem Phys 114: 8154-8158.
    • (2001) J Chem Phys , vol.114 , pp. 8154-8158
    • Favrin, G.1    Irbäck, A.2    Sjunnesson, F.3
  • 64
    • 4243819810 scopus 로고
    • New Monte Carlo technique for studying phase transitions
    • Ferrenberg AM, Swendsen RH, (1989) New Monte Carlo technique for studying phase transitions. Phys Rev Lett 61: 2635-2638.
    • (1989) Phys Rev Lett , vol.61 , pp. 2635-2638
    • Ferrenberg, A.M.1    Swendsen, R.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.