메뉴 건너뛰기




Volumn 7, Issue 1-2, 2000, Pages 183-192

Hierarchy of regions of amino acid sequence with respect to their role in the protein spatial structure

Author keywords

Hierarchy of domain structure; Interaction energy; Protein folding; Protein spatial structure; Sequence alignment

Indexed keywords

AMINO ACID SEQUENCE; GENETIC PROCEDURES; MACROMOLECULE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW; SEQUENCE HOMOLOGY;

EID: 0034101680     PISSN: 10665277     EISSN: None     Source Type: Journal    
DOI: 10.1089/10665270050081450     Document Type: Review
Times cited : (5)

References (22)
  • 3
    • 0013695651 scopus 로고    scopus 로고
    • The distribution of direct interactions in the spatial structures of globular proteins
    • Berezovskii, I.N., Esipova, N.G., and Tumanyan, V.G. 1998a. The distribution of direct interactions in the spatial structures of globular proteins. Biophysics (Biofizika, Moscow). 43, 367-377.
    • (1998) Biophysics (Biofizika, Moscow) , vol.43 , pp. 367-377
    • Berezovskii, I.N.1    Esipova, N.G.2    Tumanyan, V.G.3
  • 4
    • 0013695652 scopus 로고    scopus 로고
    • A new approach for the calculation of the energy of van der Waals interactions in globular proteins. Medium permittivity as a physical parameter for the calculation
    • Berezovskii, I.N., Esipova, N.G., Tumanyan, V.G., and Namiot, V.A. 1998b. A new approach for the calculation of the energy of van der Waals interactions in globular proteins. Medium permittivity as a physical parameter for the calculation. Biophysics (Biofizika, Moscow), 43, 909-916.
    • (1998) Biophysics (Biofizika, Moscow) , vol.43 , pp. 909-916
    • Berezovskii, I.N.1    Esipova, N.G.2    Tumanyan, V.G.3    Namiot, V.A.4
  • 5
    • 0032845660 scopus 로고    scopus 로고
    • Hierarchy of the interaction energy distribution in the spatial structure of globular proteins and the problem of domain definition
    • Berezovsky, I.N., Namiot, V.A., Tumanyan, V.G., and Esipova, N.G. 1999. Hierarchy of the interaction energy distribution in the spatial structure of globular proteins and the problem of domain definition. J. Biomol. Struct. Dyn. 17, 133-155.
    • (1999) J. Biomol. Struct. Dyn. , vol.17 , pp. 133-155
    • Berezovsky, I.N.1    Namiot, V.A.2    Tumanyan, V.G.3    Esipova, N.G.4
  • 6
    • 0000807828 scopus 로고    scopus 로고
    • Isolation of the energy-signifie ant parts of the globule and the hierarchy of the domain structure of the protein macromolecule
    • Berezovskii, I.N., Esipova, N.G., and Tumanyan, V.G. 1997a. Isolation of the energy-signifie ant parts of the globule and the hierarchy of the domain structure of the protein macromolecule. Biophysics (Biofizika, Moscow). 42, 557-565.
    • (1997) Biophysics (Biofizika, Moscow) , vol.42 , pp. 557-565
    • Berezovskii, I.N.1    Esipova, N.G.2    Tumanyan, V.G.3
  • 7
    • 0030732907 scopus 로고    scopus 로고
    • Representation of amino acid sequence in terms of interaction energy in protein globule
    • Berezovsky, I.N., Tumanyan, V.G., and Esipova, N.G. 1997b. Representation of amino acid sequence in terms of interaction energy in protein globule. FEBS Letters. 418, 43-46.
    • (1997) FEBS Letters , vol.418 , pp. 43-46
    • Berezovsky, I.N.1    Tumanyan, V.G.2    Esipova, N.G.3
  • 8
    • 0000804955 scopus 로고
    • Objective method for isolating the domains of globular proteins
    • Berezovskii, I.N., and Tumanyan, V.G. 1995. Objective method for isolating the domains of globular proteins. Biophysics (Biofizika, Moscow). 40, 1181-1187.
    • (1995) Biophysics (Biofizika, Moscow) , vol.40 , pp. 1181-1187
    • Berezovskii, I.N.1    Tumanyan, V.G.2
  • 9
    • 0027122748 scopus 로고
    • One thousand families for the molecular biologist
    • Chothia, C. 1992. One thousand families for the molecular biologist. Nature. 357, 543-544.
    • (1992) Nature , vol.357 , pp. 543-544
    • Chothia, C.1
  • 10
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K.A. 1990. Dominant forces in protein folding. Biochemistry. 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 12
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch, Z.S., and Tidor, B. 1994. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Science, 3, 211-226.
    • (1994) Protein Science , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 13
    • 0027991446 scopus 로고
    • The FSSP database of structurally aligned fold families
    • Holm, L., and Sander, C. 1994. The FSSP database of structurally aligned fold families. Nucl. Acids Res. 22, 3600-3609.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 14
    • 0025663105 scopus 로고
    • Strength and co-operativity of contributions of surface salt bridges to protein stability
    • Horovitz, A., Serrano, L., Avron, B., Bycroft, M., and Fersht, A.R. 1990. Strength and co-operativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216, 1031-1044.
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 15
    • 0028891784 scopus 로고
    • Identification and analysis of domains in proteins
    • Islam, S.A., Luo, J., and Sternberg, M.J.E. 1995. Identification and analysis of domains in proteins. Protein Engineering 8, 513-525.
    • (1995) Protein Engineering , vol.8 , pp. 513-525
    • Islam, S.A.1    Luo, J.2    Sternberg, M.J.E.3
  • 16
    • 0029843132 scopus 로고    scopus 로고
    • Hydrogen bonding stabilizes globular proteins
    • Myers, J.K., and Pace, C.N. 1996. Hydrogen bonding stabilizes globular proteins. Biophysical J. 71, 2033-2039.
    • (1996) Biophysical J. , vol.71 , pp. 2033-2039
    • Myers, J.K.1    Pace, C.N.2
  • 17
    • 33845550595 scopus 로고
    • Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbounded interactions, and hydrogen bond interactions for the naturally occuring amino acids
    • Nemethy, G., Pottle, M.S., and Sheraga, H.A. 1983. Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbounded interactions, and hydrogen bond interactions for the naturally occuring amino acids. J. Phys. Chem. 87, 1883-1887.
    • (1983) J. Phys. Chem. , vol.87 , pp. 1883-1887
    • Nemethy, G.1    Pottle, M.S.2    Sheraga, H.A.3
  • 18
    • 0028593509 scopus 로고
    • Protein superfamilies and domain superfolds
    • Orengo, C.A., Jones, D.T., and Thornton, J.M. 1994 Protein superfamilies and domain superfolds. Nature, 372, 631-634.
    • (1994) Nature , vol.372 , pp. 631-634
    • Orengo, C.A.1    Jones, D.T.2    Thornton, J.M.3
  • 19
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace, C.N., Shirley, B.A., McNutt, M., and Gajiwala, K. 1996. Forces contributing to the conformational stability of proteins. FASEB J. 10, 75-83.
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 20
    • 0028081403 scopus 로고
    • Structural features can be unconserved in proteins with similar folds. An analysis of side-chain to side-chain contacts, secondary structure and accessibility
    • Russel, R.B., and Barton G.J. 1994. Structural features can be unconserved in proteins with similar folds. An analysis of side-chain to side-chain contacts, secondary structure and accessibility. J. Mol. Biol. 244, 332-350.
    • (1994) J. Mol. Biol. , vol.244 , pp. 332-350
    • Russel, R.B.1    Barton, G.J.2
  • 21
    • 0031566432 scopus 로고    scopus 로고
    • Recognition of analogous and homologous protein folds: Analysis of sequnce and structure conservation
    • Russel, R.B., Saqi, M.A.S., Sayle, R.A., Bates, P.A., and Sternberg, M.J.E. 1997. Recognition of analogous and homologous protein folds: Analysis of sequnce and structure conservation. J. Mol. Biol. 269, 423-439.
    • (1997) J. Mol. Biol. , vol.269 , pp. 423-439
    • Russel, R.B.1    Saqi, M.A.S.2    Sayle, R.A.3    Bates, P.A.4    Sternberg, M.J.E.5
  • 22
    • 0028943588 scopus 로고
    • Continuous and discontinuous domains: An algorithm for the automatic generation of reliable protein domain definition
    • Siddiqui, A.S., and Barton, G.J. 1995. Continuous and discontinuous domains: An algorithm for the automatic generation of reliable protein domain definition. Protein Science 4, 872-884.
    • (1995) Protein Science , vol.4 , pp. 872-884
    • Siddiqui, A.S.1    Barton, G.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.