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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-termi...

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Sonraí Bibleagrafaíochta
Main Authors: Kurapkat, G., De Wolf, E., Grötzinger, J., Wollmer, A.
Formáid: Artigo
Teanga:Inglês
Foilsithe: Cold Spring Harbor Laboratory Press 1997
Ábhair:
Rochtain Ar Líne:https://ncbi.nlm.nih.gov/pmc/articles/PMC2143665/
https://ncbi.nlm.nih.gov/pubmed/9070440
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