Tendamistat (12–26) fragment

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  • NMR characterization of isolated β‐turn folding intermediates

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<jats:p>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 α‐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 β turn exists in the native protein. Such a set of structures are destabilized when one residue located within the native β turn of the 15–23 peptide is modified Trp 18→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.</jats:p>

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