메뉴 건너뛰기




Volumn 10, Issue 6, 2001, Pages 1172-1177

Environmental features are important in determining protein secondary structure

Author keywords

Prediction secondary structure; Protein folding

Indexed keywords

AMINO ACID; PROTEIN; SOLVENT;

EID: 0035018354     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.420101     Document Type: Article
Times cited : (26)

References (23)
  • 1
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou, P.Y. and Fasman, G.D. 1978. Empirical predictions of protein conformation. Ann. Rev. Biochem. 47: 251-276.
    • (1978) Ann. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 2
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly, M.L. 1983. Analytical molecular surface calculation. J. Appl. Cryst. 16: 548-558.
    • (1983) J. Appl. Cryst. , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 3
    • 0033106244 scopus 로고    scopus 로고
    • Evaluation and improvement of multiple sequence methods for protein secondary structure prediction
    • Cuff, J.A. and Barton, G.J. 1999. Evaluation and improvement of multiple sequence methods for protein secondary structure prediction. Proteins Struct. Funct. Genet. 34: 508-519.
    • (1999) Proteins Struct. Funct. Genet. , vol.34 , pp. 508-519
    • Cuff, J.A.1    Barton, G.J.2
  • 4
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., Osguthorpe, D.J., and Robson, B. 1978. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120: 97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 6
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Garnier, J., Gibrat, J.F., and Robson B. 1996. GOR method for predicting protein secondary structure from amino acid sequence. Meth. Enzymol. 266: 540-553.
    • (1996) Meth. Enzymol. , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 7
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm, U. and Sander, C. 1994. Enlarged representative set of protein structures. Protein Sci. 3: 522-524.
    • (1994) Protein Sci. , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 8
    • 0000268209 scopus 로고
    • Protein secondary structure prediction with a neural network
    • Holley, L.H. and Karplus, M. 1989. Protein secondary structure prediction with a neural network. Proc. Natl. Acad. Sci. 86: 152-156.
    • (1989) Proc. Natl. Acad. Sci. , vol.86 , pp. 152-156
    • Holley, L.H.1    Karplus, M.2
  • 9
    • 0033562619 scopus 로고    scopus 로고
    • Assigning secondary structure from protein coordinate data
    • King, S.M. and Johnson, W.C. 1999. Assigning secondary structure from protein coordinate data. Proteins Struct. Funct. Genet. 35: 313-320.
    • (1999) Proteins Struct. Funct. Genet. , vol.35 , pp. 313-320
    • King, S.M.1    Johnson, W.C.2
  • 10
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graphics 14: 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 11
    • 0034192637 scopus 로고    scopus 로고
    • The relative order of helical propensity of amino acids changes with solvent environment
    • Krittanai, C. and Johnson, W.C., Jr. 2000. The relative order of helical propensity of amino acids changes with solvent environment. Proteins Struct. Funct. Genet. 39: 132-141.
    • (2000) Proteins Struct. Funct. Genet. , vol.39 , pp. 132-141
    • Krittanai, C.1    Johnson W.C., Jr.2
  • 12
    • 0023050277 scopus 로고
    • An algorithm for secondary structure determination in proteins based on sequence simulation
    • Levin, J.M., Robson, B., and Gamier, J. 1986. An algorithm for secondary structure determination in proteins based on sequence simulation. FASEB Lett. 205: 303-308.
    • (1986) FASEB Lett. , vol.205 , pp. 303-308
    • Levin, J.M.1    Robson, B.2    Gamier, J.3
  • 13
    • 0030904568 scopus 로고    scopus 로고
    • A direct comparison of helix propensity in proteins and peptides
    • Myers, J.K., Pace, C.N., and Scholtz, J.M. 1997. A direct comparison of helix propensity in proteins and peptides. Proc. Natl. Acad. Sci. 94: 2833-2837.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 2833-2837
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 14
    • 0022495251 scopus 로고
    • Amino acid sequence homolog applied to the prediction of protein secondary structure, and joint prediction with existing methods
    • Nishikawa, K. and Ooi, T. 1986. Amino acid sequence homolog applied to the prediction of protein secondary structure, and joint prediction with existing methods. Biochim. Biophys. Acta 871: 45-54.
    • (1986) Biochim. Biophys. Acta , vol.871 , pp. 45-54
    • Nishikawa, K.1    Ooi, T.2
  • 15
    • 0021988059 scopus 로고
    • Prediction of homology and divergence in the secondary structure of polypeptides
    • Pongor, S. and Szaley, A.A. 1985. Prediction of homology and divergence in the secondary structure of polypeptides. Proc. Natl. Acad. Sci. 82: 366-370.
    • (1985) Proc. Natl. Acad. Sci. , vol.82 , pp. 366-370
    • Pongor, S.1    Szaley, A.A.2
  • 16
    • 0023803244 scopus 로고
    • Predicting the secondary structure of globular proteins using neural network models
    • Qian, N. and Sejnowski, T.J. 1988. Predicting the secondary structure of globular proteins using neural network models. J. Mol. Biol. 202: 865-884.
    • (1988) J. Mol. Biol. , vol.202 , pp. 865-884
    • Qian, N.1    Sejnowski, T.J.2
  • 17
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B. and Sander, C. 1993. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232: 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 18
    • 0026682530 scopus 로고
    • Predicting protein secondary structure using neural net and statistical methods
    • Stolorz, P., Lapedes, A., and Xia, Y. 1992. Predicting protein secondary structure using neural net and statistical methods. J. Mol. Biol. 225: 363-377.
    • (1992) J. Mol. Biol. , vol.225 , pp. 363-377
    • Stolorz, P.1    Lapedes, A.2    Xia, Y.3
  • 19
    • 0022761233 scopus 로고
    • Evolutionary similarity among peptide segments is a basis for prediction of protein folding
    • Sweet, R.M. 1986. Evolutionary similarity among peptide segments is a basis for prediction of protein folding. Biopolymers 25: 1565-1577.
    • (1986) Biopolymers , vol.25 , pp. 1565-1577
    • Sweet, R.M.1
  • 20
    • 0028279006 scopus 로고
    • Importance of environment in determining secondary structure in proteins
    • Waterhous, D.V. and Johnson, W.C., Jr. 1994. Importance of environment in determining secondary structure in proteins. Biochemistry 33: 2121-2128.
    • (1994) Biochemistry , vol.33 , pp. 2121-2128
    • Waterhous, D.V.1    Johnson W.C., Jr.2
  • 22
    • 0026608073 scopus 로고
    • Environment affects amino acid preference for secondary structure
    • Zhong, L. and Johnson, W.C., Jr. 1992. Environment affects amino acid preference for secondary structure. Proc. Natl. Acad. Sci. 89: 4462-4465.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 4462-4465
    • Zhong, L.1    Johnson W.C., Jr.2
  • 23
    • 0023660653 scopus 로고
    • Prediction of protein secondary structure and active sites using alignment of homologous sequence
    • Zvelebil, M.J., Barton, G.J., Taylor, W.R., and Sternberg, M.J.E. 1987. Prediction of protein secondary structure and active sites using alignment of homologous sequence. J. Mol. Biol. 194: 957-961.
    • (1987) J. Mol. Biol. , vol.194 , pp. 957-961
    • Zvelebil, M.J.1    Barton, G.J.2    Taylor, W.R.3    Sternberg, M.J.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.