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Volumn 316, Issue 3, 2002, Pages 799-805

Motifs of serine and threonine can drive association of transmembrane helices

Author keywords

Association; Hydrogen bond; Membrane protein; Protein folding; TOXCAT

Indexed keywords

GLYCINE; HYDROXYL GROUP; SERINE; THREONINE;

EID: 0036301006     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5353     Document Type: Article
Times cited : (219)

References (28)
  • 8
    • 0031956790 scopus 로고    scopus 로고
    • The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues
    • (1998) Protein Sci. , vol.7 , pp. 1052-1056
    • Brosig, B.1    Langosch, D.2
  • 9
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions
    • (2000) J. Mol. Biol. , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 18
    • 0021755525 scopus 로고
    • Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins
    • (1984) J. Mol. Biol. , vol.175 , pp. 75-81
    • Gray, T.M.1    Matthews, B.W.2
  • 25


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.