메뉴 건너뛰기




Volumn 12, Issue 7, 2003, Pages 1406-1417

Analysis of accessible surface of residues in proteins

Author keywords

Amphipathy; Hydrophobicity; Pex files; Secondary structure; Solvent accessibility

Indexed keywords

AMINO ACID; PROTEIN; SOLVENT;

EID: 0038309560     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0304803     Document Type: Article
Times cited : (199)

References (22)
  • 1
    • 0025936242 scopus 로고
    • Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations
    • Brasseur, R. 1991. Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations. J. Biol. Chem. 266: 16120-16127.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16120-16127
    • Brasseur, R.1
  • 2
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surfaces in proteins
    • Chothia, C. 1976. The nature of the accessible and buried surfaces in proteins. J. Mol. Biol. 105: 1-12.
    • (1976) J. Mol. Biol. , vol.105 , pp. 1-12
    • Chothia, C.1
  • 3
    • 0030939096 scopus 로고    scopus 로고
    • Disposition of amphiphilic helices in heteropolar environments
    • Chou, K.C., Zhang, C.T., and Maggiora, G.M. 1997. Disposition of amphiphilic helices in heteropolar environments. Proteins 28: 99-108.
    • (1997) Proteins , vol.28 , pp. 99-108
    • Chou, K.C.1    Zhang, C.T.2    Maggiora, G.M.3
  • 4
    • 0001880425 scopus 로고
    • Chemical properties of polypeptides
    • ed. T. Creighton. W.H. Freeman and Company, New York
    • Creighton, T. 1993. Chemical properties of polypeptides. In Chemical properties of polypeptides (ed. T. Creighton), pp. 1-46. W.H. Freeman and Company, New York.
    • (1993) Chemical Properties of Polypeptides , pp. 1-46
    • Creighton, T.1
  • 5
    • 0030462271 scopus 로고    scopus 로고
    • Hydrophobic regions on protein surfaces: Definition based on hydration shell structure and a quick method for their computation
    • Eisenhaber, F. and Argos, P. 1996. Hydrophobic regions on protein surfaces: Definition based on hydration shell structure and a quick method for their computation. Protein Eng. 9: 1121-1133.
    • (1996) Protein Eng. , vol.9 , pp. 1121-1133
    • Eisenhaber, F.1    Argos, P.2
  • 6
    • 0031410522 scopus 로고    scopus 로고
    • SERF: A program for accessible surface area calculations
    • Flower, D.R. 1997. SERF: A program for accessible surface area calculations. J. Mol. Graph. Model. 15: 238-244.
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 238-244
    • Flower, D.R.1
  • 7
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • Jones, S. and Thornton, J.M. 1997. Analysis of protein-protein interaction sites using surface patches. J. Mol. Biol. 272: 121-132.
    • (1997) J. Mol. Biol. , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 8
    • 0033040551 scopus 로고    scopus 로고
    • An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments
    • Li, L., Darden, T.A., Bartolotti, L., Kominos, D., and Pedersen, L.G. 1999. An atomic model for the pleated β-sheet structure of Aβ amyloid protofilaments. Biophys. J. 76: 2871-2878.
    • (1999) Biophys. J. , vol.76 , pp. 2871-2878
    • Li, L.1    Darden, T.A.2    Bartolotti, L.3    Kominos, D.4    Pedersen, L.G.5
  • 9
    • 0035189668 scopus 로고    scopus 로고
    • New method for accurate prediction of solvent accessibility from protein sequence
    • Li, X. and Pan, X.M. 2001. New method for accurate prediction of solvent accessibility from protein sequence. Proteins 42: 1-5.
    • (2001) Proteins , vol.42 , pp. 1-5
    • Li, X.1    Pan, X.M.2
  • 10
    • 0033406884 scopus 로고    scopus 로고
    • Prediction of protein secondary structure content
    • Liu, W. and Chou, K.C. 1999. Prediction of protein secondary structure content. Protein Eng. 12: 1041-1050.
    • (1999) Protein Eng. , vol.12 , pp. 1041-1050
    • Liu, W.1    Chou, K.C.2
  • 11
    • 0035283141 scopus 로고    scopus 로고
    • Prediction of protein surface accessibility with information theory
    • Naderi-Manesh, H., Sadeghi, M., Arab, S., and Moosavi Movahedi, A.A. 2001. Prediction of protein surface accessibility with information theory. Proteins 42: 452-459.
    • (2001) Proteins , vol.42 , pp. 452-459
    • Naderi-Manesh, H.1    Sadeghi, M.2    Arab, S.3    Moosavi Movahedi, A.A.4
  • 12
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profilebased neural networks
    • Rost, B. 1996. PHD: Predicting one-dimensional protein structure by profilebased neural networks. Methods Enzymol. 266: 525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 13
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • Rost, B. and Sander, C. 1994. Conservation and prediction of solvent accessibility in protein families. Proteins 20: 216-226.
    • (1994) Proteins , vol.20 , pp. 216-226
    • Rost, B.1    Sander, C.2
  • 14
    • 0036700020 scopus 로고    scopus 로고
    • Quantifying the accessible surface area of protein residues in their local environment
    • Samanta, U., Bahadur, R.P., and Chakrabarti, P. 2002. Quantifying the accessible surface area of protein residues in their local environment. Protein Eng. 15: 659-667.
    • (2002) Protein Eng. , vol.15 , pp. 659-667
    • Samanta, U.1    Bahadur, R.P.2    Chakrabarti, P.3
  • 15
    • 0032796425 scopus 로고    scopus 로고
    • Amyloid-β-sheet formation at the air-water interface
    • Schladitz, C., Vieira, E.P., Hermel, H., and Mohwald, H. 1999. Amyloid-β-sheet formation at the air-water interface. Biophys. J. 77: 3305-3310.
    • (1999) Biophys. J. , vol.77 , pp. 3305-3310
    • Schladitz, C.1    Vieira, E.P.2    Hermel, H.3    Mohwald, H.4
  • 16
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms. Lysozyme and insulin
    • Shrake, A. and Rupley, J.A. 1973. Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J. Mol. Biol. 79: 351-371.
    • (1973) J. Mol. Biol. , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2
  • 17
    • 0029055313 scopus 로고
    • LINUS: A hierarchic procedure to predict the fold of a protein
    • Srinivasan, R. and Rose, G.D. 1995. LINUS: A hierarchic procedure to predict the fold of a protein. Proteins 22: 81-99.
    • (1995) Proteins , vol.22 , pp. 81-99
    • Srinivasan, R.1    Rose, G.D.2
  • 19
    • 0035314074 scopus 로고    scopus 로고
    • Pex, analytical tools for PDB files. I. GF-Pex: Basic file to describe a protein
    • Thomas, A., Bouffioux, O., Geeurickx, D., and Brasseur, R. 2001. Pex, analytical tools for PDB files. I. GF-Pex: Basic file to describe a protein. Proteins 43: 28-36.
    • (2001) Proteins , vol.43 , pp. 28-36
    • Thomas, A.1    Bouffioux, O.2    Geeurickx, D.3    Brasseur, R.4
  • 20
    • 0036721382 scopus 로고    scopus 로고
    • Aromatic side-chain interactions in proteins. I. Main structural features
    • Thomas, A., Meurisse, R., Charloteaux, B., and Brasseur, R. 2002a. Aromatic side-chain interactions in proteins. I. Main structural features. Proteins 48: 628-634.
    • (2002) Proteins , vol.48 , pp. 628-634
    • Thomas, A.1    Meurisse, R.2    Charloteaux, B.3    Brasseur, R.4
  • 21
    • 0036721415 scopus 로고    scopus 로고
    • Aromatic side-chain interactions in proteins. II. Near- and far-sequence Phe-X pairs
    • Thomas, A., Meurisse, R., and Brasseur, R. 2002b. Aromatic side-chain interactions in proteins. II. Near- and far-sequence Phe-X pairs. Proteins 48: 635-644.
    • (2002) Proteins , vol.48 , pp. 635-644
    • Thomas, A.1    Meurisse, R.2    Brasseur, R.3
  • 22
    • 0037103004 scopus 로고    scopus 로고
    • Prediction of protein solvent accessibility using support vector machines
    • Yuan, Z., Burrage, K., and Mattick, J.S. 2002. Prediction of protein solvent accessibility using support vector machines. Proteins 48: 566-570.
    • (2002) Proteins , vol.48 , pp. 566-570
    • Yuan, Z.1    Burrage, K.2    Mattick, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.