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

Institute of Chemistry

The Hebrew University of Jerusalem

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

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

All Science Journal Classification (ASJC) codes

Electronic, Optical and Magnetic Materials
General Chemistry
Ceramics and Composites
Metals and Alloys
Materials Chemistry
Surfaces, Coatings and Films
Catalysis

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10.1039/c4cc03195d

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title = "Effect of salt on the formation of salt-bridges in β-hairpin peptides",

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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doi = "10.1039/c4cc03195d",

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AU - Sukenik, Shahar

AU - Boyarski, Yoav

AU - Harries, Daniel

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N2 - 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.

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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U2 - 10.1039/c4cc03195d

DO - 10.1039/c4cc03195d

M3 - مقالة

C2 - 24926740

SN - 1359-7345

VL - 50

SP - 8193

EP - 8196

JO - Chemical Communications

JF - Chemical Communications

IS - 60

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

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