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

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 indica...

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Bibliographic Details
Published in:Biopolymers 2003-10, Vol.70 (2), p.221-226
Main Authors: Kumashiro, Kristin K., Kurano, Tracie L., Niemczura, Walter P., Martino, Marica, Tamburro, Antonio M.
Format: Article
Language:English
Subjects:
13C chemical shifts
Animals
Carbon - chemistry
Circular Dichroism
elastin
Elastin - chemistry
elastin peptide
Magnetic Resonance Spectroscopy - methods
Peptides - chemistry
Protein Conformation
solid-state NMR
spectral editing
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Summary: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
ISSN:0006-3525
1097-0282
DOI:10.1002/bip.10470