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Volumn 342, Issue 5, 2004, Pages 1487-1504

Distinguishing structural and functional restraints in evolution in order to identify interaction sites

Author keywords

environment specific substitution tables; evolution; functional sites; protein function

Indexed keywords

AMINO ACID; PROTEIN;

EID: 4544230537     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.08.022     Document Type: Article
Times cited : (93)

References (70)
  • 1
    • 0023305986 scopus 로고
    • Knowledge-based prediction of protein structures and the design of novel molecules
    • T.L. Blundell, B.L. Sibanda, M.J. Sternberg, and J.M. Thornton Knowledge-based prediction of protein structures and the design of novel molecules Nature 326 1987 347 352
    • (1987) Nature , vol.326 , pp. 347-352
    • Blundell, T.L.1    Sibanda, B.L.2    Sternberg, M.J.3    Thornton, J.M.4
  • 2
    • 0031787022 scopus 로고    scopus 로고
    • 100,000 Protein structures for the biologist
    • A. Sali 100,000 protein structures for the biologist Nature Struct. Biol. 5 1998 1029 1032
    • (1998) Nature Struct. Biol. , vol.5 , pp. 1029-1032
    • Sali, A.1
  • 5
    • 0031690080 scopus 로고    scopus 로고
    • Automatic extraction of keywords from scientific text: Application to the knowledge domain of protein families
    • M.A. Andrade, and A. Valencia Automatic extraction of keywords from scientific text: application to the knowledge domain of protein families Bioinformatics 14 1998 600 607
    • (1998) Bioinformatics , vol.14 , pp. 600-607
    • Andrade, M.A.1    Valencia, A.2
  • 9
    • 0031766401 scopus 로고    scopus 로고
    • HOMSTRAD: A database of protein structure alignments for homologous families
    • K. Mizuguchi, C.M. Deane, T.L. Blundell, and J.P. Overington HOMSTRAD: a database of protein structure alignments for homologous families Protein Sci. 7 1998 2469 2471
    • (1998) Protein Sci. , vol.7 , pp. 2469-2471
    • Mizuguchi, K.1    Deane, C.M.2    Blundell, T.L.3    Overington, J.P.4
  • 10
    • 0033548460 scopus 로고    scopus 로고
    • Three-dimensional structure analysis of PROSITE patterns
    • A. Kasuya, and J.M. Thornton Three-dimensional structure analysis of PROSITE patterns J. Mol. Biol. 286 1999 1673 1691
    • (1999) J. Mol. Biol. , vol.286 , pp. 1673-1691
    • Kasuya, A.1    Thornton, J.M.2
  • 11
    • 0032475938 scopus 로고    scopus 로고
    • Functional analysis of the Escherichia coli genome using the sequence-to-structure-to-function paradigm: Identification of proteins exhibiting the glutaredoxin/thioredoxin disulfide oxidoreductase activity
    • J.S. Fetrow, A. Godzik, and J. Skolnick Functional analysis of the Escherichia coli genome using the sequence-to-structure-to-function paradigm: identification of proteins exhibiting the glutaredoxin/thioredoxin disulfide oxidoreductase activity J. Mol. Biol. 282 1998 703 711
    • (1998) J. Mol. Biol. , vol.282 , pp. 703-711
    • Fetrow, J.S.1    Godzik, A.2    Skolnick, J.3
  • 13
    • 0032932490 scopus 로고    scopus 로고
    • From fold predictions to function predictions: Automation of functional site conservation analysis for functional genome predictions
    • B. Zhang, L. Rychlewski, K. Pawlowski, J.S. Fetrow, J. Skolnick, and A. Godzik From fold predictions to function predictions: automation of functional site conservation analysis for functional genome predictions Protein Sci. 8 1999 1104 1115
    • (1999) Protein Sci. , vol.8 , pp. 1104-1115
    • Zhang, B.1    Rychlewski, L.2    Pawlowski, K.3    Fetrow, J.S.4    Skolnick, J.5    Godzik, A.6
  • 14
    • 0035059281 scopus 로고    scopus 로고
    • Genomic-scale comparison of sequence- and structure-based methods of functional prediction: Does structure provide additional insight?
    • J.S. Fetrow, N. Siew, J.A. Di Gennaro, M. Martinez-Yamout, H.J. Dyson, and J. Skolnick Genomic-scale comparison of sequence- and structure-based methods of functional prediction: does structure provide additional insight? Protein Sci. 10 2001 1005 1014
    • (2001) Protein Sci. , vol.10 , pp. 1005-1014
    • Fetrow, J.S.1    Siew, N.2    Di Gennaro, J.A.3    Martinez-Yamout, M.4    Dyson, H.J.5    Skolnick, J.6
  • 16
    • 0026055156 scopus 로고
    • Analysis of the steric strain in the polypeptide backbone of protein molecules
    • O. Herzberg, and J. Moult Analysis of the steric strain in the polypeptide backbone of protein molecules Proteins: Struct. Funct. Genet. 11 1991 223 229
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 223-229
    • Herzberg, O.1    Moult, J.2
  • 17
    • 0033215221 scopus 로고    scopus 로고
    • Strain in protein structures as viewed through non-rotameric side chains: II. Effects upon ligand binding
    • J. Heringa, and P. Argos Strain in protein structures as viewed through non-rotameric side chains: II. Effects upon ligand binding Proteins: Struct. Funct. Genet. 37 1999 44 55
    • (1999) Proteins: Struct. Funct. Genet. , vol.37 , pp. 44-55
    • Heringa, J.1    Argos, P.2
  • 18
    • 0035965145 scopus 로고    scopus 로고
    • Prediction of functionally important residues based solely on the computed energetics of protein structrue
    • A.H. Elcock Prediction of functionally important residues based solely on the computed energetics of protein structrue J. Mol. Biol. 213 2001 885 896
    • (2001) J. Mol. Biol. , vol.213 , pp. 885-896
    • Elcock, A.H.1
  • 19
    • 0344405703 scopus 로고    scopus 로고
    • Prediction of catalytic residues in enzymes based on known tertiary structure, stability profile and sequence conservation
    • M. Ota, K. Kinoshita, and K. Nishikawa Prediction of catalytic residues in enzymes based on known tertiary structure, stability profile and sequence conservation J. Mol. Biol. 327 2003 1053 1064
    • (2003) J. Mol. Biol. , vol.327 , pp. 1053-1064
    • Ota, M.1    Kinoshita, K.2    Nishikawa, K.3
  • 21
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • S. Jones, and J.M. Thornton Analysis of protein-protein interaction sites using surface patches J. Mol. Biol. 272 1997 121 132
    • (1997) J. Mol. Biol. , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 22
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • B. Honig, and A. Nicholls Classical electrostatics in biology and chemistry Science 268 1995 1144 1149
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 23
    • 0029775624 scopus 로고    scopus 로고
    • Cluster of charged residues in protein three-dimensional structures
    • Z.-y. Zhu, and S. Karlin Cluster of charged residues in protein three-dimensional structures Proc. Natl Acad. Sci. 93 1996 8350 8355
    • (1996) Proc. Natl Acad. Sci. , vol.93 , pp. 8350-8355
    • Zhu, Z.-Y.1    Karlin, S.2
  • 24
    • 0035838976 scopus 로고    scopus 로고
    • Automated structure-based prediction of functional sites in proteins: Applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking
    • P. Aloy, E. Querol, F.X. Aviles, and M.J.E. Sternberg Automated structure-based prediction of functional sites in proteins: applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking J. Mol. Biol. 311 2001 395 408
    • (2001) J. Mol. Biol. , vol.311 , pp. 395-408
    • Aloy, P.1    Querol, E.2    Aviles, F.X.3    Sternberg, M.J.E.4
  • 25
    • 0037470573 scopus 로고    scopus 로고
    • Annotating nucleic acid-binding function based on protein structure
    • E.W. Stawiski, L.M. Gregoret, and Y. Mandel-Gutfreund Annotating nucleic acid-binding function based on protein structure J. Mol. Biol. 326 2003 1065 1079
    • (2003) J. Mol. Biol. , vol.326 , pp. 1065-1079
    • Stawiski, E.W.1    Gregoret, L.M.2    Mandel-Gutfreund, Y.3
  • 26
    • 0023660653 scopus 로고
    • Prediction of protein secondary structure and active sites using the alignment of homologous sequences
    • M.J. Zvelebil, G.J. Barton, W.R. Taylor, and M.J. Sternberg Prediction of protein secondary structure and active sites using the alignment of homologous sequences J. Mol. Biol. 195 1987 957 961
    • (1987) J. Mol. Biol. , vol.195 , pp. 957-961
    • Zvelebil, M.J.1    Barton, G.J.2    Taylor, W.R.3    Sternberg, M.J.4
  • 27
    • 0035815113 scopus 로고    scopus 로고
    • Evolution of function in protein superfamilies, from a structural perspective
    • A.E. Todd, C.A. Orengo, and J.M. Thornton Evolution of function in protein superfamilies, from a structural perspective J. Mol. Biol. 307 2001 1113 1143
    • (2001) J. Mol. Biol. , vol.307 , pp. 1113-1143
    • Todd, A.E.1    Orengo, C.A.2    Thornton, J.M.3
  • 30
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • C. Chothia, and A.M. Lesk The relation between the divergence of sequence and structure in proteins EMBO 5 1986 823 826
    • (1986) EMBO , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 32
    • 0029913807 scopus 로고    scopus 로고
    • The evolutionary trace method defines the binding surfaces common to a protein family
    • O. Lichtarge, H.R. Bourne, and F.E. Cohen The evolutionary trace method defines the binding surfaces common to a protein family J. Mol. Biol. 257 1996 342 358
    • (1996) J. Mol. Biol. , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 33
    • 0031555477 scopus 로고    scopus 로고
    • Identification of functional surfaces of the zinc binding domains of intracellular receptors
    • O. Lichtarge, K.R. Yamamoto, and F.E. Cohen Identification of functional surfaces of the zinc binding domains of intracellular receptors J. Mol. Biol. 274 1997 325 337
    • (1997) J. Mol. Biol. , vol.274 , pp. 325-337
    • Lichtarge, O.1    Yamamoto, K.R.2    Cohen, F.E.3
  • 34
    • 0036300444 scopus 로고    scopus 로고
    • Structural clusters of evolutionary trace residues are statistically significant and common in proteins
    • S. Madabushi, H. Yao, M. Marsh, D. Kristensen, A. Philippi, M.E. Sowa, and O. Lichtarge Structural clusters of evolutionary trace residues are statistically significant and common in proteins J. Mol. Biol. 316 2002 139 154
    • (2002) J. Mol. Biol. , vol.316 , pp. 139-154
    • Madabushi, S.1    Yao, H.2    Marsh, M.3    Kristensen, D.4    Philippi, A.5    Sowa, M.E.6    Lichtarge, O.7
  • 35
    • 0037423759 scopus 로고    scopus 로고
    • An accurate, sensitive and scalable method to identify functional sites in protein structures
    • H. Yao, D.M. Kristensen, I. Mihalek, M.E. Sowa, C. Shaw, and M. Kimmel An accurate, sensitive and scalable method to identify functional sites in protein structures J. Mol. Biol. 326 2003 255 261
    • (2003) J. Mol. Biol. , vol.326 , pp. 255-261
    • Yao, H.1    Kristensen, D.M.2    Mihalek, I.3    Sowa, M.E.4    Shaw, C.5    Kimmel, M.6
  • 36
    • 0036468670 scopus 로고    scopus 로고
    • Evolutionary predictions of binding surfaces and interactions
    • O. Lichtarge, and M.A. Sowa Evolutionary predictions of binding surfaces and interactions Curr. Opin. Struct. Biol. 12 2002 12 27
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 12-27
    • Lichtarge, O.1    Sowa, M.A.2
  • 37
    • 0035896024 scopus 로고    scopus 로고
    • ConSurf: An algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information
    • A. Armon, A. Graur, and N. Ben-Tal ConSurf: an algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information J. Mol. Biol. 307 2001 447 463
    • (2001) J. Mol. Biol. , vol.307 , pp. 447-463
    • Armon, A.1    Graur, A.2    Ben-Tal, N.3
  • 38
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • T. Pupko, R.E. Bell, I. Mayrose, F. Glaser, and N. Ben-Tal Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues Bioinformatics 18 2002 S71 S77
    • (2002) Bioinformatics , vol.18
    • Pupko, T.1    Bell, R.E.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 39
    • 0035853280 scopus 로고    scopus 로고
    • Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins
    • R. Landgraf, I. Xenarios, and D. Eisenberg Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins J. Mol. Biol. 307 2001 1487 1502
    • (2001) J. Mol. Biol. , vol.307 , pp. 1487-1502
    • Landgraf, R.1    Xenarios, I.2    Eisenberg, D.3
  • 40
    • 0031897589 scopus 로고    scopus 로고
    • Predicting functions from protein sequences - Where are the bottlenecks?
    • P. Bork, and E.V. Koonin Predicting functions from protein sequences - where are the bottlenecks? Nature Genet. 18 1998 313 318
    • (1998) Nature Genet. , vol.18 , pp. 313-318
    • Bork, P.1    Koonin, E.V.2
  • 41
    • 0031797096 scopus 로고    scopus 로고
    • What we do not know about sequence analysis and sequence databases
    • P. Karp What we do not know about sequence analysis and sequence databases Bioinformatics 14 1998 753 754
    • (1998) Bioinformatics , vol.14 , pp. 753-754
    • Karp, P.1
  • 42
    • 0027062943 scopus 로고
    • Environment-specific amino acid substitution tables: Tertiary templates and prediction of protein folds
    • J. Overington, D. Donnelly, M.S. Johnson, A. Sali, and T.L. Blundell Environment-specific amino acid substitution tables: tertiary templates and prediction of protein folds Protein Sci. 1 1992 216 226
    • (1992) Protein Sci. , vol.1 , pp. 216-226
    • Overington, J.1    Donnelly, D.2    Johnson, M.S.3    Sali, A.4    Blundell, T.L.5
  • 43
    • 0025104478 scopus 로고
    • Tertiary structural constraints on protein evolutionary diversity: Templates, key residues and structure prediction
    • J. Overington, M.S. Johnson, A. Sali, and T.L. Blundell Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction Proc. R. Soc. Lond. B: Biol. Sci. 241 1990 132 145
    • (1990) Proc. R. Soc. Lond. B: Biol. Sci. , vol.241 , pp. 132-145
    • Overington, J.1    Johnson, M.S.2    Sali, A.3    Blundell, T.L.4
  • 44
    • 0028685354 scopus 로고
    • A generalized profile syntax for biomolecular sequence motifs and its function in automatic sequence interpretation
    • P. Burcher, and A. Bairoch A generalized profile syntax for biomolecular sequence motifs and its function in automatic sequence interpretation Proc. Int. Conf. Intell. Syst. Mol. Biol. 2 1994 53 61
    • (1994) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.2 , pp. 53-61
    • Burcher, P.1    Bairoch, A.2
  • 45
    • 0028136929 scopus 로고
    • PROSITE: Recent developments
    • A. Bairoch, and P. Burcher PROSITE: recent developments Nucl. Acids Res. 22 1994 3626 3627
    • (1994) Nucl. Acids Res. , vol.22 , pp. 3626-3627
    • Bairoch, A.1    Burcher, P.2
  • 48
    • 0031008715 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database: Its relevance to human molecular medical research
    • A. Bairoch, and R. Apweiler The SWISS-PROT protein sequence database: its relevance to human molecular medical research J. Mol. Med. 75 1997 312 316
    • (1997) J. Mol. Med. , vol.75 , pp. 312-316
    • Bairoch, A.1    Apweiler, R.2
  • 49
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database programs
    • S.F. Altschul, and D.J. Lipman Gapped BLAST and PSI-BLAST: a new generation of protein database programs Nucl. Acid Res. 25 1997 3389 3402
    • (1997) Nucl. Acid Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Lipman, D.J.2
  • 50
    • 0021767550 scopus 로고
    • The active site of aspartic proteinases
    • L.H. Pearl, and T.L. Blundell The active site of aspartic proteinases FEBS Letters 174 1984 96 101
    • (1984) FEBS Letters , vol.174 , pp. 96-101
    • Pearl, L.H.1    Blundell, T.L.2
  • 51
    • 0033555285 scopus 로고    scopus 로고
    • Structural basis of substrate specificity in malate dehydrogenases: Crystal structure of a ternary complex of procine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydroNAD
    • A.D.M. Chapman, A. Cortes, T.R. Dafforn, A.R. Clarke, and R.L. Brady Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of procine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydroNAD J. Mol. Biol. 285 1999 703 712
    • (1999) J. Mol. Biol. , vol.285 , pp. 703-712
    • Chapman, A.D.M.1    Cortes, A.2    Dafforn, T.R.3    Clarke, A.R.4    Brady, R.L.5
  • 52
    • 0024690076 scopus 로고
    • Lactate dehydrogenase-B cDNA from the Teleost Fundulus heteroclitus: Evolutionary implications
    • D.L. Crawford, H.R. Constantino, and D.A. Powers Lactate dehydrogenase-B cDNA from the Teleost Fundulus heteroclitus: evolutionary implications Mol. Biol. Evol. 6 1989 369 383
    • (1989) Mol. Biol. Evol. , vol.6 , pp. 369-383
    • Crawford, D.L.1    Constantino, H.R.2    Powers, D.A.3
  • 53
    • 0024215070 scopus 로고
    • A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework
    • H.M. Wilks, K.W. Hart, R. Feeney, C.R. Dunn, H. Muirhead, and W.N. Chia A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework Science 242 1988 1541 1544
    • (1988) Science , vol.242 , pp. 1541-1544
    • Wilks, H.M.1    Hart, K.W.2    Feeney, R.3    Dunn, C.R.4    Muirhead, H.5    Chia, W.N.6
  • 54
    • 0034459679 scopus 로고    scopus 로고
    • Evolutionary trace analysis of TGF-beta and related growth factors: Implications for site-directed mutagenesis
    • C.A. Innis, J. Shi, and T.L. Blundell Evolutionary trace analysis of TGF-beta and related growth factors: implications for site-directed mutagenesis Protein Eng. 13 2000 839 847
    • (2000) Protein Eng. , vol.13 , pp. 839-847
    • Innis, C.A.1    Shi, J.2    Blundell, T.L.3
  • 55
    • 0016700342 scopus 로고
    • Is the evolution of insulin Darwinian or due to selectively neutral mutation?
    • T.L. Blundell, and S.P. Wood Is the evolution of insulin Darwinian or due to selectively neutral mutation? Nature 257 1975 197 203
    • (1975) Nature , vol.257 , pp. 197-203
    • Blundell, T.L.1    Wood, S.P.2
  • 56
    • 0034974365 scopus 로고    scopus 로고
    • Evolution of the insulin molecule: Insights into structure-activity and phylogenetic relationships
    • J.M. Conlon Evolution of the insulin molecule: insights into structure-activity and phylogenetic relationships Peptide 22 2001 1183 1193
    • (2001) Peptide , vol.22 , pp. 1183-1193
    • Conlon, J.M.1
  • 59
    • 0001433241 scopus 로고
    • Knowledge based modelling of homologous proteins. Part I: Three-dimensional frameworks derived from the simultaneous superposition of multiple structures
    • M.J. Sutcliffe, I. Haneef, D. Carney, and T.L. Blundell Knowledge based modelling of homologous proteins. Part I: three-dimensional frameworks derived from the simultaneous superposition of multiple structures Protein Eng. 1 1987 377 384
    • (1987) Protein Eng. , vol.1 , pp. 377-384
    • Sutcliffe, M.J.1    Haneef, I.2    Carney, D.3    Blundell, T.L.4
  • 60
    • 0000179199 scopus 로고
    • Knowledge based modelling of homologous proteins. Part II: Rules for the conformations of substituted sidechains
    • M.J. Sutcliffe, F.R.F. Hayes, and T.L. Blundell Knowledge based modelling of homologous proteins. Part II: rules for the conformations of substituted sidechains Protein Eng. 1 1987 385 392
    • (1987) Protein Eng. , vol.1 , pp. 385-392
    • Sutcliffe, M.J.1    Hayes, F.R.F.2    Blundell, T.L.3
  • 61
    • 0025317502 scopus 로고
    • Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming
    • A. Sali, and T.L. Blundell Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming J. Mol. Biol. 212 1990 403 428
    • (1990) J. Mol. Biol. , vol.212 , pp. 403-428
    • Sali, A.1    Blundell, T.L.2
  • 62
    • 0033613812 scopus 로고    scopus 로고
    • Visualizing and quantifying molecular goodness of fit: Small-probe contact dots with explicit hydrogen atoms
    • J.M. Word, S.C. Lovell, T.H. LaBean, H.C. Taylor, M.E. Zalis, and B.K. Presley Visualizing and quantifying molecular goodness of fit: small-probe contact dots with explicit hydrogen atoms J. Mol. Biol. 285 1999 1711 1733
    • (1999) J. Mol. Biol. , vol.285 , pp. 1711-1733
    • Word, J.M.1    Lovell, S.C.2    Labean, T.H.3    Taylor, H.C.4    Zalis, M.E.5    Presley, B.K.6
  • 63
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • J.M. Word, S.C. Lovell, J.S. Richardson, and D.C. Richardson Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation J. Mol. Biol. 285 1999 1735 1747
    • (1999) J. Mol. Biol. , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 66
    • 0025952277 scopus 로고
    • Divergence measures based on the Shannon entropy
    • J. Lin Divergence measures based on the Shannon entropy IEEE Trans. Inf. Theory 37 1991 145 151
    • (1991) IEEE Trans. Inf. Theory , vol.37 , pp. 145-151
    • Lin, J.1
  • 67
    • 0036307493 scopus 로고    scopus 로고
    • Within the twighlight zone: A sensitive profile-profile comparison tool based on information theory
    • G. Yona, and M. Levitt Within the twighlight zone: a sensitive profile-profile comparison tool based on information theory J. Mol. Biol. 315 2002 1257 1275
    • (2002) J. Mol. Biol. , vol.315 , pp. 1257-1275
    • Yona, G.1    Levitt, M.2
  • 68
    • 0027049243 scopus 로고
    • The kinemage: A tool for scientific illustration
    • D.C. Richardson, and J.S. Richardson The kinemage: a tool for scientific illustration Protein Sci. 1 1992 3 9
    • (1992) Protein Sci. , vol.1 , pp. 3-9
    • Richardson, D.C.1    Richardson, J.S.2
  • 69
    • 0013033189 scopus 로고    scopus 로고
    • (Rossmann, M. G., Arnold, E., eds), Kluwer Publishers, Dordrecht. Chapter 25.2.8.
    • Richardson, D. C. & Richardson, J. S. (2001). In International Tables for Crystallography (Rossmann, M. G., Arnold, E., eds), pp. 727-730, Kluwer Publishers, Dordrecht. Chapter 25.2.8.
    • (2001) International Tables for Crystallography , pp. 727-730
    • Richardson, D.C.1    Richardson, J.S.2
  • 70
    • 0345062357 scopus 로고    scopus 로고
    • Universally conserved positions in protein folds: Reading evolutionary signals about stability, folding kinetics and function
    • L.A. Mirny, and E.I. Shakhnovich Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function J. Mol. Biol. 291 1999 177 196
    • (1999) J. Mol. Biol. , vol.291 , pp. 177-196
    • Mirny, L.A.1    Shakhnovich, E.I.2


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