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Volumn 316, Issue 2, 2002, Pages 225-233

Residues participating in the protein folding nucleus do not exhibit preferential evolutionary conservation

Author keywords

Homology; Nucleation; Phi value; Sequence entropy; Two state

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; ENTROPY; EXPERIMENTAL DESIGN; KINETICS; MOLECULAR EVOLUTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; SEQUENCE HOMOLOGY; THEORETICAL STUDY;

EID: 0036295887     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5344     Document Type: Article
Times cited : (58)

References (34)
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    • How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins
    • (1980) J. Mol. Biol. , vol.136 , pp. 225-270
    • Lesk, A.M.1    Chothia, C.2
  • 21
    • 0034984382 scopus 로고    scopus 로고
    • Mapping the folding pathway of an immunoglobulin domain: Structural detail from phi value analysis and movement of the transition state
    • (2001) Structure , vol.9 , pp. 355-356
    • Fowler, S.B.1    Clarke, J.2
  • 29
    • 0032542018 scopus 로고    scopus 로고
    • Mutagenesis of a buried polar interaction in an SH3 domain: Sequence conservation provides the best prediction of stability effects
    • (1998) Biochemistry , vol.37 , pp. 16172-16182
    • Maxwell, K.L.1    Davidson, A.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.