Inactive conformation of an insulin despite its wild-type sequence
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چکیده
منابع مشابه
Inactive conformation of an insulin despite its wild-type sequence.
The peptide group between residues B24 and B25 of insulin was replaced by an ester bond. This modification only in the backbone was meant to eliminate a structurally important H-bond between the amide proton of B25 and the carbonyl oxygen of A19, and consequently to enhance detachment of the C-terminal B-chain from the body of the molecule, exposing the underlying A-chain. According to a model ...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1997
ISSN: 0961-8368
DOI: 10.1002/pro.5560060307