A synthetic resilin is largely unstructured

Nairn, Kate M., Lyons, Russell E., Mulder, Roger J., Mudie, Stephen T., Cookson, David J., Lesieur, Emmanuelle, Kim, Misook, Lau, Deborah, Schole, Fiona H. and Elvin, Christopher M. (2008) A synthetic resilin is largely unstructured. Biophysical Journal, 95 7: 3358-3365. doi:10.1529/biophysj.107.119107

Author Nairn, Kate M.
Lyons, Russell E.
Mulder, Roger J.
Mudie, Stephen T.
Cookson, David J.
Lesieur, Emmanuelle
Kim, Misook
Lau, Deborah
Schole, Fiona H.
Elvin, Christopher M.
Title A synthetic resilin is largely unstructured
Journal name Biophysical Journal   Check publisher's open access policy
ISSN 0006-3495
Publication date 2008-10-01
Sub-type Article (original research)
DOI 10.1529/biophysj.107.119107
Volume 95
Issue 7
Start page 3358
End page 3365
Total pages 8
Place of publication Bethesda, U.S.
Publisher Cell Press for the Biophysical Society
Language eng
Subject 0601 Biochemistry and Cell Biology
Formatted abstract
Proresilin is the precursor protein for resilin, an extremely elastic, hydrated, cross-linked insoluble protein found in insects. We investigated the secondary-structure distribution in solution of a synthetic proresilin (AN16), based on 16 units of the consensus proresilin repeat from Anopheles gambiae. Raman spectroscopy was used to verify that the secondary-structure distributions in cross-linked AN16 resilin and in AN16 proresilin are similar, and hence that solution techniques (such as NMR and circular dichroism) may be used to gain information about the structure of the cross-linked solid. The synthetic proresilin AN16 is an intrinsically unstructured protein, displaying under native conditions many of the characteristics normally observed in denatured proteins. There are no apparent α-helical or β-sheet features in the NMR spectra, and the majority of backbone protons and carbons exhibit chemical shifts characteristic of random-coil configurations. Relatively few peaks are observed in the nuclear Overhauser effect spectra, indicating that overall the protein is dynamic and unstructured. The radius of gyration of AN16 corresponds to the value expected for a denatured protein of similar chain length. This high degree of disorder is also consistent with observed circular dichroism and Raman spectra. The temperature dependences of the NH proton chemical shifts were also measured. Most values were indicative of protons exposed to water, although smaller dependences were observed for glycine and alanine within the Tyr-Gly-Ala-Pro sequence conserved in all resilins found to date, which is the site of dityrosine cross-link formation. This result implies that these residues are involved in hydrogen bonds, possibly to enable efficient self-association and subsequent cross-linking. The β-spiral model for elastic proteins, where the protein is itself shaped like a spring, is not supported by the results for AN16. Both the random-network elastomer model and the sliding β-turn model are consistent with the data. The results indicate a flat energy landscape for AN16, with very little energy required to switch between conformations. This ease of switching is likely to lead to the extremely low energy loss on deformation of resilin.
Q-Index Code C1
Q-Index Status Provisional Code

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 43 times in Thomson Reuters Web of Science Article | Citations
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Created: Fri, 05 Feb 2010, 15:38:06 EST by Christine Ouslinis on behalf of Institute for Molecular Bioscience