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
Biopolymersjournal_title
Biopolymersauthors
Kumashiro KK,Kurano TL,Niemczura WP,Martino M,Tamburro AMdoi
10.1002/bip.10470subject
Has Abstractpub_date
2003-10-01 00:00:00pages
221-6issue
2eissn
0006-3525issn
1097-0282journal_volume
70pub_type
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