메뉴 건너뛰기




Volumn 32, Issue 2, 1998, Pages 190-199

Easy method to predict solvent accessibility from multiple protein sequence alignments

Author keywords

Protein folding; Protein sequence; Protein structure; Protein structure prediction; Solvent accessibility

Indexed keywords

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; DATA BASE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING;

EID: 0032147008     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980801)32:2<190::AID-PROT5>3.0.CO;2-P     Document Type: Article
Times cited : (35)

References (21)
  • 1
    • 0030764671 scopus 로고    scopus 로고
    • Protein structural classes in five complete genomes
    • Frishmann, D., Mewes, H.W. Protein structural classes in five complete genomes. Nature Struct. Biol. 4:626-628, 1997.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 626-628
    • Frishmann, D.1    Mewes, H.W.2
  • 2
    • 0028815464 scopus 로고
    • Protein structure prediction: Recognition of primary, secondary, and tertiary structural features from amino acid sequence
    • Eisenhaber, F., Persson, B., Argos, P. Protein structure prediction: Recognition of primary, secondary, and tertiary structural features from amino acid sequence. Crit. Rev. Biochem. Mol. Biol. 30:1-94, 1995.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 1-94
    • Eisenhaber, F.1    Persson, B.2    Argos, P.3
  • 3
    • 0027489387 scopus 로고
    • Quantification of secondary-structure prediction improvement using multiple alignments
    • Levin, J.M., Pascarella, S., Argos, P., Gamier J. Quantification of secondary-structure prediction improvement using multiple alignments. Prot. Eng. 6:849-854, 1993.
    • (1993) Prot. Eng. , vol.6 , pp. 849-854
    • Levin, J.M.1    Pascarella, S.2    Argos, P.3    Gamier, J.4
  • 4
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B., Sander, C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55-72, 1994.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 5
    • 0028825192 scopus 로고
    • A simple and fast approach to prediction of protein secondary structure from multiply aligned sequences with accuracy above 70%
    • Mehta, P.K., Heringa, J., Argos, P. A simple and fast approach to prediction of protein secondary structure from multiply aligned sequences with accuracy above 70%. Protein Sci. 4:2517-2525, 1995.
    • (1995) Protein Sci. , vol.4 , pp. 2517-2525
    • Mehta, P.K.1    Heringa, J.2    Argos, P.3
  • 6
    • 0030931336 scopus 로고    scopus 로고
    • Seventy-five percent accuracy in protein secondary-structure prediction
    • Frishmann, D., Argos, P. Seventy-five percent accuracy in protein secondary-structure prediction. Proteins 27:329-335, 1997.
    • (1997) Proteins , vol.27 , pp. 329-335
    • Frishmann, D.1    Argos, P.2
  • 7
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B., Richards, F.M. The interpretation of protein structures: Estimation of static accessibility. J. Mol. Biol. 55:379-400, 1971.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 8
    • 0025039476 scopus 로고
    • Predicting surface exposure of amino acids from protein sequence
    • Holbrook, S.R., Muskal, S.M., Kim, S.-H. Predicting surface exposure of amino acids from protein sequence. Protein Eng. 3:659-665, 1990.
    • (1990) Protein Eng. , vol.3 , pp. 659-665
    • Holbrook, S.R.1    Muskal, S.M.2    Kim, S.-H.3
  • 9
    • 0028239337 scopus 로고
    • Use of amino acid environment-dependent substitution tables and conformational propensities in structure prediction from aligned sequences of homologous proteins. I. Solvent accessibility classes
    • Wako, H., Blundell, T.L. Use of amino acid environment-dependent substitution tables and conformational propensities in structure prediction from aligned sequences of homologous proteins. I. Solvent accessibility classes. J. Mol. Biol. 238:682-692, 1994.
    • (1994) J. Mol. Biol. , vol.238 , pp. 682-692
    • Wako, H.1    Blundell, T.L.2
  • 10
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • Rost, B., Sander, C. Conservation and prediction of solvent accessibility in protein families. Proteins 20:216-226, 1994.
    • (1994) Proteins , vol.20 , pp. 216-226
    • Rost, B.1    Sander, C.2
  • 11
    • 0029885547 scopus 로고    scopus 로고
    • Predicting solvent accessibility: Higher accuracy using Bayesian statistics and optimized residue substitution classes
    • Thompson, M.J., Goldstein, R.A. Predicting solvent accessibility: Higher accuracy using Bayesian statistics and optimized residue substitution classes. Proteins 25:38-47, 1996.
    • (1996) Proteins , vol.25 , pp. 38-47
    • Thompson, M.J.1    Goldstein, R.A.2
  • 12
    • 0023645034 scopus 로고
    • Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins
    • Cornette, J.L., Cease, K.B., Margalit, H., Spouge, J.L., Berzofsky, J.A., DeLisi, C. Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J. Mol. Biol. 195:659-685, 1987.
    • (1987) J. Mol. Biol. , vol.195 , pp. 659-685
    • Cornette, J.L.1    Cease, K.B.2    Margalit, H.3    Spouge, J.L.4    Berzofsky, J.A.5    DeLisi, C.6
  • 13
    • 0029918306 scopus 로고    scopus 로고
    • A databank (3D_ali) collecting related protein sequences and structures
    • Pascarella, S., Milpetz, F., Argos, P. A databank (3D_ali) collecting related protein sequences and structures. Protein Eng. 9:349-351, 1996.
    • (1996) Protein Eng. , vol.9 , pp. 349-351
    • Pascarella, S.1    Milpetz, F.2    Argos, P.3
  • 14
    • 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 22:2577-2637, 1983.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 15
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surface in proteins
    • Chothia, C. The nature of the accessible and buried surface in proteins. J. Mol. Biol. 105:1-14, 1976.
    • (1976) J. Mol. Biol. , vol.105 , pp. 1-14
    • Chothia, C.1
  • 16
    • 0028019234 scopus 로고
    • Navigating the Brookhaven protein databank
    • Walsh, L.L. Navigating the Brookhaven protein databank. Computer Appl. Biosci. 10:551-557, 1994.
    • (1994) Computer Appl. Biosci. , vol.10 , pp. 551-557
    • Walsh, L.L.1
  • 17
    • 0026030641 scopus 로고
    • Database of homology-derived structures and the structural meaning of sequence alignment
    • Sander, C., Schneider, R. Database of homology-derived structures and the structural meaning of sequence alignment. Proteins 9:56-68, 1991.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 18
    • 0028081403 scopus 로고
    • Structural features can be unconserved in proteins with similar folds
    • Russel, R.B., Burton, G.J. Structural features can be unconserved in proteins with similar folds. J. Mol. Biol. 244:332-350, 1994.
    • (1994) J. Mol. Biol. , vol.244 , pp. 332-350
    • Russel, R.B.1    Burton, G.J.2
  • 19
    • 0029980527 scopus 로고    scopus 로고
    • Identifying the tertiary fold of small proteins with different topologies from sequence and secondary structure using the genetic algorithm and extended criteria specific for strand regions
    • Dandekar, T., Argos, P. Identifying the tertiary fold of small proteins with different topologies from sequence and secondary structure using the genetic algorithm and extended criteria specific for strand regions. J. Mol. Biol. 256:645-660, 1996.
    • (1996) J. Mol. Biol. , vol.256 , pp. 645-660
    • Dandekar, T.1    Argos, P.2
  • 20
    • 0028297304 scopus 로고
    • Folding the mainchain of small proteins with the genetic algorithm
    • Dandekar, T., Argos, P. Folding the mainchain of small proteins with the genetic algorithm. J. Mol. Biol. 236:844-861, 1994.
    • (1994) J. Mol. Biol. , vol.236 , pp. 844-861
    • Dandekar, T.1    Argos, P.2
  • 21
    • 0023645203 scopus 로고
    • Interior and surface of monomeric proteins
    • Miller, S., Janin, J., Lesk, A.M., Chothia, C. Interior and surface of monomeric proteins. J. Mol. Biol, 196:641-656, 1987.
    • (1987) J. Mol. Biol , vol.196 , pp. 641-656
    • Miller, S.1    Janin, J.2    Lesk, A.M.3    Chothia, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.