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13 C CPMAS NMR studies of the elastin‐like polypeptide (LGGVG) n
Author(s) -
Kumashiro Kristin K.,
Kurano Tracie L.,
Niemczura Walter P.,
Martino Marica,
Tamburro Antonio M.
Publication year - 2003
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10470
Subject(s) - elastin , chemistry , peptide , biopolymer , solid state nuclear magnetic resonance , crystallography , biophysics , stereochemistry , biochemistry , polymer , nuclear magnetic resonance , organic chemistry , medicine , physics , pathology , biology
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 β‐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. © 2003 Wiley Periodicals, Inc. Biopolymers 70: 221–226, 2003