Stabilization of helical peptides by mixed spaced salt bridges

Jay S. Berger, James A. Ernst, Angelo C. Nicoletta, Leslie A. Hull, Jianxin Yang, Rong Qiu, Victor N. Morozov, Neville R. Kallenbach

Research output: Contribution to journalArticle

Abstract

Whether or not surface salt bridges have a strong stabilizing effect on the native structure in proteins remains uncertain. Previous studies of model peptides have shown that salt bridges spaced at i, i+4 along the chain are more stabilizing than those spaced at i, i+3, with a preference for the order acid-base rather than base-acid from N to C terminus. An analysis of the effect of spacing the ion pairs in short helical peptides is presented, in which acidic and basic side chains spaced two or three residues apart alternate along the chain. The mixed spacing proves to be stabilizing relative to pure spacings. A control peptide in which salt bridges were spaced uniformly three residues apart proved to form a β-sheet structure rather than a-helix. This is due to formation of a silk-like apolar face consisting of alanine side chains; the mesoscopic structure formed by these sheets can be imaged by scanning microscopy.

Original languageEnglish (US)
Pages (from-to)285-291
Number of pages7
JournalJournal of Biomolecular Structure and Dynamics
Volume14
Issue number3
DOIs
StatePublished - Dec 1996

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Berger, J. S., Ernst, J. A., Nicoletta, A. C., Hull, L. A., Yang, J., Qiu, R., Morozov, V. N., & Kallenbach, N. R. (1996). Stabilization of helical peptides by mixed spaced salt bridges. Journal of Biomolecular Structure and Dynamics, 14(3), 285-291. https://doi.org/10.1080/07391102.1996.10508124