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Volumn 33, Issue DATABASE ISS., 2005, Pages

PFD: A database for the investigation of protein folding kinetics and stability

Author keywords

[No Author keywords available]

Indexed keywords

ACCESS TO INFORMATION; ARTICLE; BIOINFORMATICS; COMPUTER INTERFACE; COMPUTER PROGRAM; INFORMATION PROCESSING; INFORMATION RETRIEVAL; INTERNET; METHODOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DATABASE; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FOLDING DATABASE; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS; HUMAN COMPUTER INTERACTION; INFORMATION SYSTEM; PROTEIN ANALYSIS; STRUCTURE ANALYSIS;

EID: 13444304369     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gki016     Document Type: Article
Times cited : (26)

References (15)
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  • 5
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    • How do small single-domain proteins fold?
    • Jackson,S.E. (1998) How do small single-domain proteins fold? Fold. Des., 3, R81-R90.
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    • Jackson, S.E.1
  • 6
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco,K.W., Simons,K.T. and Baker,D. (1998) Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol., 277, 985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 7
    • 0032708771 scopus 로고    scopus 로고
    • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
    • Chiti,F., Taddei,N., White,P.M., Bucciantini,M., Magherini,F., Stefani,M. and Dobson,C.M. (1999) Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nature Struct. Biol., 6, 1005-1009.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1005-1009
    • Chiti, F.1    Taddei, N.2    White, P.M.3    Bucciantini, M.4    Magherini, F.5    Stefani, M.6    Dobson, C.M.7
  • 8
    • 0032750509 scopus 로고    scopus 로고
    • The Folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • Martinez,J.C. and Serrano,L. (1999) The Folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nature Struct. Biol., 6, 1010-1016.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1010-1016
    • Martinez, J.C.1    Serrano, L.2
  • 10
    • 0033200251 scopus 로고    scopus 로고
    • Folding studies of the immunoglobulin-like beta-sandwich proteins suggest their share a common folding pathway
    • Clarke,J., Cota,E., Fowler,S.B. and Hamill,S.J. (1999) Folding studies of the immunoglobulin-like beta-sandwich proteins suggest their share a common folding pathway. Structure Fold. Des., 7 1145-1153.
    • (1999) Structure Fold. Des. , vol.7 , pp. 1145-1153
    • Clarke, J.1    Cota, E.2    Fowler, S.B.3    Hamill, S.J.4
  • 12
    • 2942689229 scopus 로고    scopus 로고
    • Prediction of protein folding rates from the amino acid sequence-predicted secondary structure
    • Ivankov,D.N. and Finkelstein,A.V. (2004) Prediction of protein folding rates from the amino acid sequence-predicted secondary structure. Proc. Natl Acad. Sci. USA, 101, 8942-8944.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8942-8944
    • Ivankov, D.N.1    Finkelstein, A.V.2
  • 13
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    • Unification of the folding mechanisms of non-two-state and two-state proteins
    • Kamagata,K., Arai,M. and Kuwajima,K. (2004) Unification of the folding mechanisms of non-two-state and two-state proteins. J. Mol. Biol., 339, 951-965.
    • (2004) J. Mol. Biol. , vol.339 , pp. 951-965
    • Kamagata, K.1    Arai, M.2    Kuwajima, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.