메뉴 건너뛰기




Volumn 6, Issue , 2005, Pages

A decoy set for the thermostable subdomain from chicken villin headpiece, comparison of different free energy estimators

Author keywords

[No Author keywords available]

Indexed keywords

COVALENT STRUCTURES; ENERGY MINIMIZATION; GENERALIZED BORN SURFACE AREAS (GBSA); MODEL QUALITY ESTIMATION; MOLECULAR DYNAMICS SIMULATIONS; MOLECULAR DYNAMICS TRAJECTORIES; POISSON BOLTZMANN SURFACE AREAS (PBSA); SECONDARY STRUCTURE ELEMENTS;

EID: 29244479220     PISSN: 14712105     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-6-301     Document Type: Article
Times cited : (15)

References (48)
  • 1
    • 13844291273 scopus 로고    scopus 로고
    • Protein refinement: A new challenge for CASP in its 10th anniversary
    • Valencia A: Protein refinement: a new challenge for CASP in its 10th anniversary. Bioinformatics 2005, 21:277.
    • (2005) Bioinformatics , vol.21 , pp. 277
    • Valencia, A.1
  • 2
    • 0032502803 scopus 로고    scopus 로고
    • Molecular mechanisms for cooperative folding of proteins
    • Hao M, Scheraga H: Molecular mechanisms for cooperative folding of proteins. J. Mol. Biol. 1998, 277:973-983.
    • (1998) J. Mol. Biol. , vol.277 , pp. 973-983
    • Hao, M.1    Scheraga, H.2
  • 3
    • 0033531959 scopus 로고    scopus 로고
    • Discrimination of the native from misfolded protein models with an energy function including implicit solvation
    • Lazaridis T, Karplus M: Discrimination of the native from misfolded protein models with an energy function including implicit solvation. J Mol Biol 1999, 288:477-87.
    • (1999) J Mol Biol , vol.288 , pp. 477-487
    • Lazaridis, T.1    Karplus, M.2
  • 4
    • 0034486196 scopus 로고    scopus 로고
    • Free energy determinants of tertiary structure and the evaluation of protein models
    • Petrey D, Honig B: Free energy determinants of tertiary structure and the evaluation of protein models. Protein Sci 2000, 9:2181-2191.
    • (2000) Protein Sci , vol.9 , pp. 2181-2191
    • Petrey, D.1    Honig, B.2
  • 5
    • 15244349255 scopus 로고    scopus 로고
    • Application of MM/PBSA colony free energy to loop decoy discrimination: Towards correlation between energy and root mean square deviation
    • Fogolari F, Tosatto S: Application of MM/PBSA colony free energy to loop decoy discrimination: towards correlation between energy and root mean square deviation. Prot. Sci. 2005, 14:889-901.
    • (2005) Prot. Sci. , vol.14 , pp. 889-901
    • Fogolari, F.1    Tosatto, S.2
  • 6
    • 0027650879 scopus 로고
    • Boltzmann's principle, knowledge-based mean fields and protein folding. An approach to the computational determination of protein structures
    • Sippl M: Boltzmann's principle, knowledge-based mean fields and protein folding. An approach to the computational determination of protein structures. J. Comput. Aided Mol. Des. 1993, 7:473-501.
    • (1993) J. Comput. Aided Mol. Des. , vol.7 , pp. 473-501
    • Sippl, M.1
  • 7
    • 0032488962 scopus 로고    scopus 로고
    • An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction
    • Samudrala R, Moult J: An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction. J Mol Biol 1998, 275:895-916.
    • (1998) J Mol Biol , vol.275 , pp. 895-916
    • Samudrala, R.1    Moult, J.2
  • 8
    • 0035882533 scopus 로고    scopus 로고
    • A distance-dependent atomic knowledge-based potential for improved protein structure selection
    • Lu H, Skolnick J: A distance-dependent atomic knowledge-based potential for improved protein structure selection. Proteins 2001, 44:223-232.
    • (2001) Proteins , vol.44 , pp. 223-232
    • Lu, H.1    Skolnick, J.2
  • 9
    • 0036838311 scopus 로고    scopus 로고
    • Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction
    • Zhou H, Zhou Y: Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci. 2002, 11:2714-2726.
    • (2002) Protein Sci. , vol.11 , pp. 2714-2726
    • Zhou, H.1    Zhou, Y.2
  • 10
    • 0642340510 scopus 로고    scopus 로고
    • Amino acid empirical contact energy definitions for fold recognition in the space of contact maps
    • Berrera M, Molinari H, Fogolari F: Amino acid empirical contact energy definitions for fold recognition in the space of contact maps. BMC Bioinformatics 2003, 4:8.
    • (2003) BMC Bioinformatics , vol.4 , pp. 8
    • Berrera, M.1    Molinari, H.2    Fogolari, F.3
  • 11
    • 4544355522 scopus 로고    scopus 로고
    • Improved protein structure selection using decoy-dependent discriminatory functions
    • Wang K, Fain B, Levitt M, Samudrala R: Improved protein structure selection using decoy-dependent discriminatory functions. BMC Struct. Biol. 2004, 4:8.
    • (2004) BMC Struct. Biol. , vol.4 , pp. 8
    • Wang, K.1    Fain, B.2    Levitt, M.3    Samudrala, R.4
  • 12
    • 1642534609 scopus 로고    scopus 로고
    • An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state
    • Zhang C, Liu S, Zhou H, Zhou Y: An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state. Protein Sci. 2004, 13:400-411.
    • (2004) Protein Sci. , vol.13 , pp. 400-411
    • Zhang, C.1    Liu, S.2    Zhou, H.3    Zhou, Y.4
  • 13
    • 0033853177 scopus 로고    scopus 로고
    • Decoys 'R' us: A database of incorrect protein conformations to improve protein structure prediction
    • Samudrala R, Levitt M: Decoys 'R' us: a database of incorrect protein conformations to improve protein structure prediction. Protein Sci. 2000, 9:1399-1401.
    • (2000) Protein Sci. , vol.9 , pp. 1399-1401
    • Samudrala, R.1    Levitt, M.2
  • 14
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution
    • Duan Y, Kollman P: Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution. Science 1998, 282:740-744.
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.2
  • 15
    • 4344619300 scopus 로고    scopus 로고
    • All-atom folding simulations of the Villin headpiece from stochastically-selected coarse-grained structures
    • Mori GD, Micheletti C, Colombo G: All-atom folding simulations of the Villin headpiece from stochastically-selected coarse-grained structures. J Phys Chem B 2004, 12267-12270:33.
    • (2004) J Phys Chem B , vol.33 , pp. 12267-12270
    • Mori, G.D.1    Micheletti, C.2    Colombo, G.3
  • 16
    • 11344285181 scopus 로고    scopus 로고
    • Study of the Villin headpiece folding dynamics by combining coarse-grained Monte Carlo evolution and all-atom molecular dynamics
    • Mori GD, Colombo G, Micheletti C: Study of the Villin headpiece folding dynamics by combining coarse-grained Monte Carlo evolution and all-atom molecular dynamics. Proteins 2005, 459-471:58.
    • (2005) Proteins , vol.58 , pp. 459-471
    • Mori, G.D.1    Colombo, G.2    Micheletti, C.3
  • 17
    • 0036428782 scopus 로고    scopus 로고
    • Simulation of folding of a small alpha-helical protein in atomistic detail using worldwide-distributed computing
    • Zagrovic B, Snow C, Shirts M, Pande V: Simulation of folding of a small alpha-helical protein in atomistic detail using worldwide-distributed computing. J Mol Biol 2002, 323:927-937.
    • (2002) J Mol Biol , vol.323 , pp. 927-937
    • Zagrovic, B.1    Snow, C.2    Shirts, M.3    Pande, V.4
  • 19
    • 2542462060 scopus 로고    scopus 로고
    • Folding of the villin headpiece subdomain from random structures. Analysis of the charge distribution as a function of pH
    • Ripoll D, Vila J, Scheraga, H: Folding of the villin headpiece subdomain from random structures. Analysis of the charge distribution as a function of pH. J Mol Biol 2004, 339:915-925.
    • (2004) J Mol Biol , vol.339 , pp. 915-925
    • Ripoll, D.1    Vila, J.2    Scheraga, H.3
  • 20
    • 17044382925 scopus 로고    scopus 로고
    • Free energy landscape of the villin headpiece in an all-atom force field
    • Herges T, Wenzel W: Free energy landscape of the villin headpiece in an all-atom force field. Structure 2005, 13:661-668.
    • (2005) Structure , vol.13 , pp. 661-668
    • Herges, T.1    Wenzel, W.2
  • 21
    • 0035857402 scopus 로고    scopus 로고
    • α RMSD structure predictions on two small proteins, HP-36 and s15
    • α RMSD structure predictions on two small proteins, HP-36 and s15. J. Am. Chem. Soc. 2001, 123:1040-1046.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1040-1046
    • Lee, M.R.1    Baker, D.2    Kollman, P.A.3
  • 22
    • 19644381706 scopus 로고    scopus 로고
    • High-resolution X-Ray crystal structure of the villin headpiece subdomain, an ultrafast folding protein
    • Chiu T, Kubelka J, Herbst-Irmer R, Eaton W, Hofrichter J, Davies D: High-resolution X-Ray crystal structure of the villin headpiece subdomain, an ultrafast folding protein. Proc Natl Acad Sci 2005, 102:7517-7522.
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 7517-7522
    • Chiu, T.1    Kubelka, J.2    Herbst-Irmer, R.3    Eaton, W.4    Hofrichter, J.5    Davies, D.6
  • 23
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R, MacArthur M, Moss D, Thornton J: PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst 1993, 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 24
    • 0036136694 scopus 로고    scopus 로고
    • Composites of local structure propensities: Evidence for local encoding of long range structure
    • Shortle D: Composites of local structure propensities: evidence for local encoding of long range structure. Protein Sci. 2002, 11:18-26.
    • (2002) Protein Sci. , vol.11 , pp. 18-26
    • Shortle, D.1
  • 25
    • 19544371352 scopus 로고    scopus 로고
    • A consistent set of statistical potentials for quantifying local side-chain and backbone interactions
    • Fang Q, Shortle D: A consistent set of statistical potentials for quantifying local side-chain and backbone interactions. Proteins 2005, 60:90-96.
    • (2005) Proteins , vol.60 , pp. 90-96
    • Fang, Q.1    Shortle, D.2
  • 26
    • 28144448406 scopus 로고    scopus 로고
    • The Victor/FRST Function for Model Quality Estimation
    • [In press]
    • Tosatto S: The Victor/FRST Function for Model Quality Estimation. J. Comput. Biol. 2005. [In press.].
    • (2005) J. Comput. Biol.
    • Tosatto, S.1
  • 27
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating free energies: The colony energy and its application to the problem of loop prediction
    • Xiang Z, Soto SC, Honig B: Evaluating free energies: the colony energy and its application to the problem of loop prediction. Proc. Natl. Acad. Sci. USA. 2002, 99:7432-7437.
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 7432-7437
    • Xiang, Z.1    Soto, S.C.2    Honig, B.3
  • 29
    • 33846823909 scopus 로고
    • Particle Mesh Ewald. An N.log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L: Particle Mesh Ewald. An N.log(N) method for Ewald sums in large systems. Journal of Chemical Physics 1993, 98:10089-10092.
    • (1993) Journal of Chemical Physics , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 34
    • 84986440341 scopus 로고
    • SETTLE: An analytical version of the SHAKE and RATTLE algorithms for rigid water models
    • Miyamoto S, Kollman PA: SETTLE: An analytical version of the SHAKE and RATTLE algorithms for rigid water models. J. Comp. Chem. 1992, 13:952-962.
    • (1992) J. Comp. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 35
    • 0003624584 scopus 로고
    • GRoningen MAchine for Chemical Simulations
    • Department of Biophysical Chemistry, BIOSON Research Institute, Nijenborgh 4 NL-9717 AG Groningen [E-mail to gromacsγhem.rug.nl]
    • van der Spoel D, van Drunen R, Berendsen HJC: GRoningen MAchine for Chemical Simulations. Department of Biophysical Chemistry, BIOSON Research Institute, Nijenborgh 4 NL-9717 AG Groningen 1994. [E-mail to gromacsγhem.rug.nl].
    • (1994)
    • van der Spoel, D.1    van Drunen, R.2    Berendsen, H.J.C.3
  • 38
    • 4043171970 scopus 로고    scopus 로고
    • The GB/SA Continuum Model for Solvation. A Fast Analytical Method for the Calculation of Approximate Born Radii
    • Qiu D, Shenkin P, Hollinger F, Still W: The GB/SA Continuum Model for Solvation. A Fast Analytical Method for the Calculation of Approximate Born Radii. J. Phys. Chem. 1997, 101:3005-3014.
    • (1997) J. Phys. Chem. , vol.101 , pp. 3005-3014
    • Qiu, D.1    Shenkin, P.2    Hollinger, F.3    Still, W.4
  • 39
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
    • Jones DT: GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J. Mol. Biol. 1999, 287:797-815.
    • (1999) J. Mol. Biol. , vol.287 , pp. 797-815
    • Jones, D.T.1
  • 40
    • 14644441639 scopus 로고    scopus 로고
    • MM/PBSA analysis of molecular dynamics simulations of bovine b-lactoglobulin: Free energy gradients in conformational transitions?
    • Fogolari F, Moroni E, Wojciechowski M, Baginski M, Ragona L, Molinari H: MM/PBSA analysis of molecular dynamics simulations of bovine b-lactoglobulin: free energy gradients in conformational transitions? Proteins 2005, 59:91-103.
    • (2005) Proteins , vol.59 , pp. 91-103
    • Fogolari, F.1    Moroni, E.2    Wojciechowski, M.3    Baginski, M.4    Ragona, L.5    Molinari, H.6
  • 41
    • 0036873086 scopus 로고    scopus 로고
    • The Poisson-Boltzmann equation for biomolecular electrostatics: A tool for structural biology
    • Fogolari F, Brigo A, Molinari H: The Poisson-Boltzmann equation for biomolecular electrostatics: a tool for structural biology. J. Mol. Recogn. 2002, 15:377-392.
    • (2002) J. Mol. Recogn. , vol.15 , pp. 377-392
    • Fogolari, F.1    Brigo, A.2    Molinari, H.3
  • 42
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B: Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 1991, 11:281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 43
    • 0038650794 scopus 로고    scopus 로고
    • Protocol for MM/PBSA molecular dynamics simulations of proteins
    • Fogolari F, Brigo A, Molinari H: Protocol for MM/PBSA molecular dynamics simulations of proteins. Biophys. J. 2003, 85:159-166.
    • (2003) Biophys. J. , vol.85 , pp. 159-166
    • Fogolari, F.1    Brigo, A.2    Molinari, H.3
  • 44
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner M, Spehner JC, Olson A: Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 1996, 38:305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.1    Spehner, J.C.2    Olson, A.3
  • 47
    • 0032937077 scopus 로고    scopus 로고
    • Biomolecular electrostatics with the linearized Poisson-Boltzmann equation
    • Fogolari F, Zuccato P, Esposito G, Viglino P: Biomolecular electrostatics with the linearized Poisson-Boltzmann equation. Biophys. J. 1999, 76:1-16.
    • (1999) Biophys. J. , vol.76 , pp. 1-16
    • Fogolari, F.1    Zuccato, P.2    Esposito, G.3    Viglino, P.4
  • 48
    • 0035976385 scopus 로고    scopus 로고
    • Molecular mechanics and dynamics of biomolecules using a solvent continuum model
    • Fogolari F, Esposito G, Viglino P, Molinari H: Molecular mechanics and dynamics of biomolecules using a solvent continuum model. J. Comput. Chem. 2001, 22:1830-1842.
    • (2001) J. Comput. Chem. , vol.22 , pp. 1830-1842
    • Fogolari, F.1    Esposito, G.2    Viglino, P.3    Molinari, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.