Order, Disorder, and Temperature-Driven Compaction in a Designed Elastin Protein.

ABSTRACT: Artificial minielastin constructs have been designed that replicate the structure and function of natural elastins in a simpler context, allowing the NMR observation of structure and dynamics of elastin-like proteins with complete residue-specific resolution. We find that the alanine-rich cross-linking domains of elastin have a partially helical structure, but only when capped by proline-rich hydrophobic domains. We also find that the hydrophobic domains, composed of prominent 6-residue repeats VPGVGG and APGVGV found in natural elastins, appear random coil by both NMR chemical shift analysis and circular dichroism. However, these elastin hydrophobic domains exhibit structural bias for a dynamically disordered conformation that is neither helical nor β sheet with a degree of nonrandom stru

SUBMITTER: Greenland KN 

PROVIDER: S-EPMC6588176 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature