Tendamistat (12-26) fragment. NMR characterization of isolated beta-turn folding inte
 

Tendamistat (12-26) fragment. NMR characterization of isolated beta-turn folding intermediates.

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Eur J Biochem. 1991 Sep 1;200(2):345-51

Authors: Blanco FJ, Jiménez MA, Rico M, Santoro J, Herranz J, Nieto JL

In order to determine whether regions of a protein that are turns in the native structure are able to maintain such a structure when isolated, we have studied the conformational properties of various peptide fragments corresponding to the 12-26-peptide region of the alpha-amylase inhibitor tendamistat, by NMR. Amide solvent accessibility, NOE spectroscopy (NOESY) and rotating-frame NOE spectroscopy (ROESY) data strongly support the conclusion that the 12-26 and 15-23 peptides adopt in aqueous solution, a set of turn-like structures located around the central region of their corresponding polypeptidic chains, the same region where a beta turn exists in the native protein. Such a set of structures are destabilized when one residue located within the native beta turn of the 15-23 peptide is modified Trp18----Ser. Our results indicate that the tendency to bend in a predetermined region of a protein chain seems to exist from the very beginning of the folding process and therefore it could drive the folding instead of being a consequence of the tertiary assembly of the protein.

PMID: 1889403 [PubMed - indexed for MEDLINE]



Source: PubMed