This Article Full Text Full Text (PDF) All Versions of this Article: biophysj.106.100339v1 92/8/2885    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lefèvre, T. Articles by Pézolet, M. Search for Related Content PubMed PubMed Citation Articles by Lefèvre, T. Articles by Pézolet, M.

Protein Secondary Structure and Orientation in Silk as Revealed by Raman Spectromicroscopy

Centre de Recherche en Sciences et Ingénierie des Macromolécules, Centre de Recherche sur la Fonction, la Structure et l'Ingénierie des Protéines, Département de Chimie, Université Laval, Pavillon Alexandre-Vachon, Québec, Canada

Correspondence: Address reprint requests to Michel Pézolet, Département de Chimie, Université Laval, Pavillon Alexandre-Vachon, Québec G1K 7P4, Canada. Tel.: 418-656-2481; Fax: 418-656-7916; E-mail: michel.pezolet{at}chm.ulaval.ca.

Taking advantage of recent advances in polarized Raman microspectroscopy, and based on a rational decomposition of the amide I band, the conformation and orientation of proteins have been determined for cocoon silks of the silkworms Bombyx mori and Samia cynthia ricini and dragline silks of the spiders Nephila clavipes and Nephila edulis. This study distinguished between band components due to ß-sheets, ß-turns, 3₁-helices, and unordered structure for the four fibers. For B. mori, the ß-sheet content is 50%, which matches the proportion of residues that form the GAGAGS fibroin motifs. For the Nephila dragline and S. c. ricini cocoon, the ß-sheet content (36–37% and 45%, respectively) is higher than the proportion of residues that belong to polyalanine blocks (18% and 42%, respectively), showing that adjacent GGA motifs are incorporated into the ß-sheets. Nephila spidroins contain fewer ß-sheets and more flexible secondary structures than silkworm fibroins. The amorphous polypeptide chains are preferentially aligned parallel to the fiber direction, although their level of orientation is much lower than that of ß-sheets. Overall, the results show that the four silks exhibit a common molecular organization, with mixtures of different amounts of ß-sheets and flexible structures, which are organized with specific orientation levels.

This article has been cited by other articles:

				S. Rammensee, U. Slotta, T. Scheibel, and A. R. Bausch From the Cover: Assembly mechanism of recombinant spider silk proteins PNAS, May 6, 2008; 105(18): 6590 - 6595. [Abstract] [Full Text] [PDF]