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Protein Science (2004), 13:1134-1147. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Factors involved in the stability of isolated {beta}-sheets: Turn sequence, {beta}-sheet twisting, and hydrophobic surface burial

Clara M. Santiveri1, Jorge Santoro, Manuel Rico and M. Angeles Jiménez

Instituto de Química-Física Rocasolano, Consejo Superior de Investigaciones Científicas, 28006 Madrid, Spain

(RECEIVED November 18, 2003; FINAL REVISION January 15, 2004; ACCEPTED January 20, 2004)



Abstract

We have recently reported on the design of a 20-residue peptide able to form a significant population of a three-stranded up-and-down antiparallel {beta}-sheet in aqueous solution. To improve our {beta}-sheet model in terms of the folded population, we have modified the sequences of the two 2-residue turns by introducing the segment DPro-Gly, a sequence shown to lead to more rigid type II' {beta}-turns. The analysis of several NMR parameters, NOE data, as well as {Delta}{delta}C{alpha}H, {Delta}{delta}C{beta}, and {Delta}{delta}C{beta} values, demonstrates that the new peptide forms a {beta}-sheet structure in aqueous solution more stable than the original one, whereas the substitution of the DPro residues by LPro leads to a random coil peptide. This agrees with previous results on {beta}-hairpin-forming peptides showing the essential role of the turn sequence for {beta}-hairpin folding. The well-defined {beta}-sheet motif calculated for the new designed peptide (pair-wise RMSD for backbone atoms is 0.5 ± 0.1 Å) displays a high degree of twist. This twist likely contributes to stability, as a more hydrophobic surface is buried in the twisted {beta}-sheet than in a flatter one. The twist observed in the up-and-down antiparallel {beta}-sheet motifs of most proteins is less pronounced than in our designed peptide, except for the WW domains. The additional hydrophobic surface burial provided by {beta}-sheet twisting relative to a "flat" {beta}-sheet is probably more important for structure stability in peptides and small proteins like the WW domains than in larger proteins for which there exists a significant contribution to stability arising from their extensive hydrophobic cores.

Keywords: NMR; {beta}-turn; {beta}-sheet stability; {beta}-sheet structure; {beta}-sheet twist; peptide design

Reprint requests to: M. Angeles Jiménez, Instituto de Química-Física Rocasolano, Consejo Superior de Investigaciones Científicas, Serrano 119, 28006 Madrid, Spain; e-mail: majimenez{at}iqfr.csic.es; fax: 34-91-5642431.

Supplemental material: See www.proteinscience.org

1 Present address: MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 2QH, UK.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03520704.


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