Intramolecular cross-linked insulin

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The conformational stability and flexibility of insulin with an additional intramolecular cross-link.

The conformational stability and flexibility of insulin containing a cross-link between the alpha-amino group of the A-chain to the epsilon-amino group of Lys29 of the B-chain was examined. The cross-link varied in length from 2 to 12 carbon atoms. The conformational stability was determined by guanidine hydrochloride-induced equilibrium denaturation and flexibility was assessed by H2O/D2O amid...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 1972

ISSN: 0014-5793

DOI: 10.1016/0014-5793(72)80175-3