Effect of salt on the formation of salt-bridges in β-hairpin peptides

Shahar Sukenik; Yoav Boyarski; Daniel Harries

doi:10.1039/c4cc03195d

Effect of salt on the formation of salt-bridges in β-hairpin peptides

Shahar Sukenik
, Yoav Boyarski
, Daniel Harries^*

^*Corresponding author for this work

Institute of Chemistry

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Salt-bridges ubiquitously form between oppositely charged moieties in proteins. Here we quantify changes in population of salt-bridged β-hairpin peptides due to added salt, and determine the thermodynamic driving forces and cooperativity of salt-bridge formation under these conditions. We find only a fraction of salt-bridged folded conformations at physiologically relevant salt concentrations.

Original language	English
Pages (from-to)	8193-8196
Number of pages	4
Journal	Chemical Communications
Volume	50
Issue number	60
DOIs	https://doi.org/10.1039/c4cc03195d
State	Published - 1 Jul 2014

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10.1039/c4cc03195d

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abstract = "Salt-bridges ubiquitously form between oppositely charged moieties in proteins. Here we quantify changes in population of salt-bridged β-hairpin peptides due to added salt, and determine the thermodynamic driving forces and cooperativity of salt-bridge formation under these conditions. We find only a fraction of salt-bridged folded conformations at physiologically relevant salt concentrations.",

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AB - Salt-bridges ubiquitously form between oppositely charged moieties in proteins. Here we quantify changes in population of salt-bridged β-hairpin peptides due to added salt, and determine the thermodynamic driving forces and cooperativity of salt-bridge formation under these conditions. We find only a fraction of salt-bridged folded conformations at physiologically relevant salt concentrations.

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Effect of salt on the formation of salt-bridges in β-hairpin peptides

Abstract

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