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Volumn 99, Issue 2, 2002, Pages 189-198

Influence of medium- and long-range interactions in different folding types of globular proteins

Author keywords

Folds; Long range contacts; Medium range contacts; Structural class

Indexed keywords

AMINO ACID; DNA; GLOBULAR PROTEIN; RIBONUCLEASE; RNA;

EID: 0037120763     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00183-7     Document Type: Article
Times cited : (13)

References (36)
  • 1
    • 0027122748 scopus 로고
    • Proteins. One thousand families for the molecular biologist
    • Chothia C. Proteins. One thousand families for the molecular biologist. Nature. 357:1992;543-544.
    • (1992) Nature , vol.357 , pp. 543-544
    • Chothia, C.1
  • 2
    • 0028325958 scopus 로고
    • On the conformational stability of folded proteins
    • Ponnuswamy P.K., Gromiha M.M. On the conformational stability of folded proteins. J. Theor. Biol. 166:1994;63-74.
    • (1994) J. Theor. Biol. , vol.166 , pp. 63-74
    • Ponnuswamy, P.K.1    Gromiha, M.M.2
  • 3
    • 0030832809 scopus 로고    scopus 로고
    • Short-range conformational energies, secondary structure propensities, and recognition of correct sequence-structure matches
    • Bahar, Kaplan M., Jernigan R.L. Short-range conformational energies, secondary structure propensities, and recognition of correct sequence-structure matches. Proteins. 29:1997;309-317.
    • (1997) Proteins , vol.29 , pp. 309-317
    • Bahar1    Kaplan, M.2    Jernigan, R.L.3
  • 4
    • 0030945036 scopus 로고    scopus 로고
    • Consistency in structural energetics of protein folding and peptide recognition
    • Zhang C., Cornette J.L., Delisi C. Consistency in structural energetics of protein folding and peptide recognition. Protein Sci. 6:1997;1057-1064.
    • (1997) Protein Sci. , vol.6 , pp. 1057-1064
    • Zhang, C.1    Cornette, J.L.2    Delisi, C.3
  • 5
    • 18344412919 scopus 로고    scopus 로고
    • Analysis of hydrophobic and charged patches and influence of medium and long range interactions in molecular chaperones
    • Kumarevel T.S., Gromiha M.M., Ponnuswamy M.N. Analysis of hydrophobic and charged patches and influence of medium and long range interactions in molecular chaperones. Biophys. Chem. 75:1998;105-113.
    • (1998) Biophys. Chem. , vol.75 , pp. 105-113
    • Kumarevel, T.S.1    Gromiha, M.M.2    Ponnuswamy, M.N.3
  • 6
    • 0031909873 scopus 로고    scopus 로고
    • Recognition of analogous and homologous protein folds - Assessment of prediction success and associated alignment accuracy using empirical substitution matrices
    • Russell R.B., Saqi M.A., Sayle P.A., Sternberg M.J. Recognition of analogous and homologous protein folds - assessment of prediction success and associated alignment accuracy using empirical substitution matrices. Protein Engg. 11:1998;1-9.
    • (1998) Protein Engg. , vol.11 , pp. 1-9
    • Russell, R.B.1    Saqi, M.A.2    Sayle, P.A.3    Sternberg, M.J.4
  • 7
    • 0032773941 scopus 로고    scopus 로고
    • Role of structural and sequence information in the prediction of protein stability changes: Comparison between buried and partially buried mutations
    • Gromiha M.M., Oobatake M., Kono H., Uedaira H., Sarai A. Role of structural and sequence information in the prediction of protein stability changes: comparison between buried and partially buried mutations. Protein Engg. 12:1999;557-561.
    • (1999) Protein Engg. , vol.12 , pp. 557-561
    • Gromiha, M.M.1    Oobatake, M.2    Kono, H.3    Uedaira, H.4    Sarai, A.5
  • 8
    • 0002559869 scopus 로고    scopus 로고
    • Inter-residue interactions in the structure, folding and stability of proteins
    • Gromiha M.M., Selvaraj S. Inter-residue interactions in the structure, folding and stability of proteins. Recent Res. Devel. Biophys. Chem. 1:2000;1-14.
    • (2000) Recent Res. Devel. Biophys. Chem. , vol.1 , pp. 1-14
    • Gromiha, M.M.1    Selvaraj, S.2
  • 9
    • 0026992556 scopus 로고
    • Nonlocal interactions stabilize compact folding intermediates in reduced unfolded bovine pancreatic trypsin inhibitor
    • Gottfried D.S., Hass E. Nonlocal interactions stabilize compact folding intermediates in reduced unfolded bovine pancreatic trypsin inhibitor. Biochemistry. 31:1992;12353-12362.
    • (1992) Biochemistry , vol.31 , pp. 12353-12362
    • Gottfried, D.S.1    Hass, E.2
  • 10
    • 0032979568 scopus 로고    scopus 로고
    • Importance of long-range interactions in protein folding
    • Gromiha M.M., Selvaraj S. Importance of long-range interactions in protein folding. Biophys. Chem. 77:1999;49-68.
    • (1999) Biophys. Chem. , vol.77 , pp. 49-68
    • Gromiha, M.M.1    Selvaraj, S.2
  • 11
    • 0028342488 scopus 로고
    • A statistical analysis of side-chain conformations in proteins: Comparison with ECEPP predictions
    • Nayeem A., Scheraga H.A. A statistical analysis of side-chain conformations in proteins: comparison with ECEPP predictions. J. Protein Chem. 13:1994;283-296.
    • (1994) J. Protein Chem. , vol.13 , pp. 283-296
    • Nayeem, A.1    Scheraga, H.A.2
  • 12
    • 0030781040 scopus 로고    scopus 로고
    • Residue-residue mean-force potentials for protein structure recognition
    • Reva B., Finkelstein A.V., Sanner M., Olson A.J. Residue-residue mean-force potentials for protein structure recognition. Protein Engg. 10:1997;865-876.
    • (1997) Protein Engg. , vol.10 , pp. 865-876
    • Reva, B.1    Finkelstein, A.V.2    Sanner, M.3    Olson, A.J.4
  • 13
    • 0031575423 scopus 로고    scopus 로고
    • MONSSTER: A method for folding globular proteins with a small number of distance constraints
    • Skolinick J., Kolinski A., Ortiz A.R. MONSSTER: a method for folding globular proteins with a small number of distance constraints. J. Mol. Biol. 265:1997;217-241.
    • (1997) J. Mol. Biol. , vol.265 , pp. 217-241
    • Skolinick, J.1    Kolinski, A.2    Ortiz, A.R.3
  • 14
    • 0029155772 scopus 로고
    • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding
    • Abkevich V.I., Gutin A.M., Shakhnovich E.I. Impact of local and non-local interactions on thermodynamics and kinetics of protein folding. J. Mol. Biol. 252:1995;460-471.
    • (1995) J. Mol. Biol. , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 15
    • 0032080921 scopus 로고    scopus 로고
    • Relatioships between protein sequence and structure patterns based on residue contacts
    • Selbig J., Argos P. Relatioships between protein sequence and structure patterns based on residue contacts. Proteins. 31:1998;172-185.
    • (1998) Proteins , vol.31 , pp. 172-185
    • Selbig, J.1    Argos, P.2
  • 16
    • 0035967862 scopus 로고    scopus 로고
    • Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: Application of long-range order to folding rate prediction
    • Gromiha M.M., Selvaraj S. Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: application of long-range order to folding rate prediction. J. Mol. Biol. 310:2001;27-32.
    • (2001) J. Mol. Biol. , vol.310 , pp. 27-32
    • Gromiha, M.M.1    Selvaraj, S.2
  • 17
    • 0001614001 scopus 로고    scopus 로고
    • Influence of medium and long-range interactions in different structural classes of globular proteins
    • Gromiha M.M., Selvaraj S. Influence of medium and long-range interactions in different structural classes of globular proteins. J. Biol. Phys. 23:1997;151-162.
    • (1997) J. Biol. Phys. , vol.23 , pp. 151-162
    • Gromiha, M.M.1    Selvaraj, S.2
  • 18
    • 0031800191 scopus 로고    scopus 로고
    • Protein secondary structure prediction in different structural classes
    • Gromiha M.M., Selvaraj S. Protein secondary structure prediction in different structural classes. Protein Engg. 11:1998;249-251.
    • (1998) Protein Engg. , vol.11 , pp. 249-251
    • Gromiha, M.M.1    Selvaraj, S.2
  • 19
    • 0035913416 scopus 로고    scopus 로고
    • Role of medium and long-range interactions in discriminating globular and membrane proteins
    • Gromiha M.M., Selvaraj S. Role of medium and long-range interactions in discriminating globular and membrane proteins. Int. J. Biol. Macromol. 29:2001;25-34.
    • (2001) Int. J. Biol. Macromol. , vol.29 , pp. 25-34
    • Gromiha, M.M.1    Selvaraj, S.2
  • 20
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and structural meaning of sequence alignment
    • Sander C., Schneider R. Database of homology-derived protein structures and structural meaning of sequence alignment. Proteins. 9:1991;56-58.
    • (1991) Proteins , vol.9 , pp. 56-58
    • Sander, C.1    Schneider, R.2
  • 22
    • 0027485083 scopus 로고
    • Comparison of conformational characteristics in structurally similar protein pairs
    • Flores T.P., Orengo C.A., Moss D., Thornton J.M. Comparison of conformational characteristics in structurally similar protein pairs. Protein Sci. 2:1993;1811-1826.
    • (1993) Protein Sci. , vol.2 , pp. 1811-1826
    • Flores, T.P.1    Orengo, C.A.2    Moss, D.3    Thornton, J.M.4
  • 23
    • 0027363912 scopus 로고
    • Structural relationships of homologous proteins as a fundamental principle in homology modeling proteins
    • Hilbert M., Bohm G., Jaenicke R. Structural relationships of homologous proteins as a fundamental principle in homology modeling proteins. Proteins. 17:1993;138-151.
    • (1993) Proteins , vol.17 , pp. 138-151
    • Hilbert, M.1    Bohm, G.2    Jaenicke, R.3
  • 24
    • 0028961335 scopus 로고
    • SCOP: A structural classification of protein database for the investigation of sequence and structures
    • Murzin A.G., Brenner S.E., Hubbard T., Chothia C. SCOP: a structural classification of protein database for the investigation of sequence and structures. J. Mol. Biol. 247:1995;536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 25
    • 0022631926 scopus 로고
    • The folding type of a protein is relevant to the amino acid composition
    • Nakashima H., Nishikawa K., Ooi T. The folding type of a protein is relevant to the amino acid composition. J. Biochem. 99:1986;153-162.
    • (1986) J. Biochem. , vol.99 , pp. 153-162
    • Nakashima, H.1    Nishikawa, K.2    Ooi, T.3
  • 26
    • 0022777472 scopus 로고
    • Prediction of protein structural class from amino acid sequence
    • Klein P., Delisi C. Prediction of protein structural class from amino acid sequence. Biopolymers. 25:1986;1659-1672.
    • (1986) Biopolymers , vol.25 , pp. 1659-1672
    • Klein, P.1    Delisi, C.2
  • 27
    • 0029051959 scopus 로고
    • A novel approach to predicting protein structural classes in a (20-1)-D amino acid composition space
    • Chou K.C. A novel approach to predicting protein structural classes in a (20-1)-D amino acid composition space. Proteins. 21:1995;319-344.
    • (1995) Proteins , vol.21 , pp. 319-344
    • Chou, K.C.1
  • 28
    • 0034141493 scopus 로고    scopus 로고
    • How good is prediction of protein structural class by the component-coupled method?
    • Wang Z.X., Yuan Z. How good is prediction of protein structural class by the component-coupled method? Proteins. 38:2000;165-175.
    • (2000) Proteins , vol.38 , pp. 165-175
    • Wang, Z.X.1    Yuan, Z.2
  • 31
    • 0032926060 scopus 로고    scopus 로고
    • The CATH database provides insights into protein structure/function relationships
    • Orengo C.A., Pearl F.M.G., Bray J.E., et al. The CATH database provides insights into protein structure/function relationships. Nucleic Acids Res. 27:1999;275-279.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 275-279
    • Orengo, C.A.1    Pearl, F.M.G.2    Bray, J.E.3
  • 32
    • 0017588168 scopus 로고
    • A study of the preferred environment of amino acid residues in globular proteins
    • Manavalan P., Ponnuswamy P.K. A study of the preferred environment of amino acid residues in globular proteins. Arch. Biochem. Biophys. 184:1977;476-487.
    • (1977) Arch. Biochem. Biophys. , vol.184 , pp. 476-487
    • Manavalan, P.1    Ponnuswamy, P.K.2
  • 33
    • 0018077908 scopus 로고
    • Hydrophobic character of amino acid residues in globular proteins
    • Manavalan P., Ponnuswamy P.K. Hydrophobic character of amino acid residues in globular proteins. Nature. 275:1978;673-674.
    • (1978) Nature , vol.275 , pp. 673-674
    • Manavalan, P.1    Ponnuswamy, P.K.2
  • 34
    • 0027354210 scopus 로고
    • Hydrophobic characteristics of folded proteins
    • Ponnuswamy P.K. Hydrophobic characteristics of folded proteins. Prog. Biophys. Mol. Biol. 59:1993;57-103.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 57-103
    • Ponnuswamy, P.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.