Conformationally assisted protein ligation using C-terminal thioester peptides [14]

Journal of the American Chemical Society

Volumn 121, Issue 26, 1999, Pages 6332-6333

  Beligere, Gangamani S ^a   Dawson, Philip E ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN;

CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; DISULFIDE BOND; LETTER; PROTEIN CONFORMATION; PROTEIN FOLDING; STRUCTURE ANALYSIS;

EID: 0033532889     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9907919     Document Type: Letter

References (28)

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14. It has recently been demonstrated that ligation reactions can generate X-Cys sites where X is any amino acid except Pro. Additionally Thr, Val, and Ile give slow (>48 h) ligation rates. Hackeng, T. M.; Griffin, J. H.; Dawson, P. E. submitted for publication, Proc. Natl. Acad. Sci. U.S.A.
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