13C CPMAS NMR studies of the elastin-like polypeptide (LGGVG)n.

Abstract:

:The elucidation of structure-function relationships in insoluble elastin is often approached using elastin-like polypeptides. In this manner, the characterization of the different regions in this extensive biopolymer may be facilitated in a "piece-wise" manner. Our solid-state NMR experiments indicate that (LGGVG)n has structural similarities to elastin and some elastin peptides, providing support for the utility of the mimetic peptides. Furthermore, previous NMR and CD studies indicated that the structure of the elastin-like polypeptide (LGGVG)n in solution is best described as a "conformational ensemble" with a mixture of type I and II beta-turns, in addition to unfolded regions. Our data indicate that the peptide does not adopt a single conformation in the solid state, lending further support to models for elastin that involve significant conformational heterogeneity.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Kumashiro KK,Kurano TL,Niemczura WP,Martino M,Tamburro AM

doi

10.1002/bip.10470

subject

Has Abstract

pub_date

2003-10-01 00:00:00

pages

221-6

issue

2

eissn

0006-3525

issn

1097-0282

journal_volume

70

pub_type

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