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Volumn 4, Issue 3, 1997, Pages 217-225

Current limitations to protein threading approaches

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; CONFERENCE PAPER; DIAGNOSTIC APPROACH ROUTE; HYDROPHILICITY; HYDROPHOBICITY; PREDICTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE; STATISTICAL ANALYSIS;

EID: 0030740445     PISSN: 10665277     EISSN: None     Source Type: Journal    
DOI: 10.1089/cmb.1997.4.217     Document Type: Conference Paper
Times cited : (34)

References (2)
  • 1
    • 0030003048 scopus 로고    scopus 로고
    • Multiple domain protein diagnostic patterns
    • Adams, R.M., Das, S., and Smith, T.F. 1996. Multiple domain protein diagnostic patterns. Protein Science 5, 1240-1249.
    • (1996) Protein Science , vol.5 , pp. 1240-1249
    • Adams, R.M.1    Das, S.2    Smith, T.F.3
  • 2
    • 0027318317 scopus 로고
    • An empirical energy function for threading protein sequence through the folding motif
    • Bryant, S.H. and Lawrence, C.E. 1993. An empirical energy function for threading protein sequence through the folding motif. Proteins: Struct. Func. Genet. 16, 92-112.
    • (1993) Proteins: Struct. Func. Genet. , vol.16 , pp. 92-112
    • Bryant, S.H.1    Lawrence, C.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.