Abstract
Calcitonin gene-related peptide (CGRP) is an intrinsically disordered, 37 residue neuropeptide that acts as a potent vasodilator. It is a member of the calcitonin peptide (Ct) family, together with amylin, calcitonin and adrenomedullin. Understanding how sequence and solvent variations affect the conformation and dynamics of these genetically and functionally related IDPs is of considerable interest. We use a nanosecond-resolved spectroscopic technique based on tryptophan triplet quenching by cystine to detect transient tertiary contact formation in CGRP under varying solvent and temperature conditions. Using this technique, we had previously found that electrostatic interactions modulate the degree of compaction in CGRP1. Here we explore the effect of solvent on CGRP structure and dynamics. We find that, though disordered, CGRP is very sensitive to small variations in the solution environment. Our findings can be rationalized in terms of polymer models and residual secondary structure content.1 Sara M. Sizemore et al. 2013 Biophys. J, Supplement, Abstract.
Published Version
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