Peptide conformations are restricted by solution stability

John S. Perkyns, Bernard Pettitt

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Thermodynamic stability and statistical mechanical theory are applied to a model of a zwitterionic tripeptide of sequence Gly-Ala-Gly in high-concentration NaCl solution. It is found that many peptide conformations cannot exist in equilibrium with the salt-water solvent as a single liquid phase. This suggests a single explanation for salting proteins into and out of solution, unique biologically active protein structures, and small energy differences between denatured and folded states, while also implying a mechanism for the resolution to the Levinthal paradox.

Original languageEnglish (US)
Pages (from-to)1-2
Number of pages2
JournalJournal of Physical Chemistry®
Volume99
Issue number1
StatePublished - 1995
Externally publishedYes

Fingerprint

Peptides
peptides
Conformations
proteins
Proteins
Saline water
paradoxes
liquid phases
Thermodynamic stability
salts
thermodynamics
Liquids
water
energy

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

Cite this

Peptide conformations are restricted by solution stability. / Perkyns, John S.; Pettitt, Bernard.

In: Journal of Physical Chemistry®, Vol. 99, No. 1, 1995, p. 1-2.

Research output: Contribution to journalArticle

@article{c2f78124fd794b1cad0267d15efaf37f,
title = "Peptide conformations are restricted by solution stability",
abstract = "Thermodynamic stability and statistical mechanical theory are applied to a model of a zwitterionic tripeptide of sequence Gly-Ala-Gly in high-concentration NaCl solution. It is found that many peptide conformations cannot exist in equilibrium with the salt-water solvent as a single liquid phase. This suggests a single explanation for salting proteins into and out of solution, unique biologically active protein structures, and small energy differences between denatured and folded states, while also implying a mechanism for the resolution to the Levinthal paradox.",
author = "Perkyns, {John S.} and Bernard Pettitt",
year = "1995",
language = "English (US)",
volume = "99",
pages = "1--2",
journal = "Journal of Physical Chemistry",
issn = "0022-3654",
publisher = "American Chemical Society",
number = "1",

}

TY - JOUR

T1 - Peptide conformations are restricted by solution stability

AU - Perkyns, John S.

AU - Pettitt, Bernard

PY - 1995

Y1 - 1995

N2 - Thermodynamic stability and statistical mechanical theory are applied to a model of a zwitterionic tripeptide of sequence Gly-Ala-Gly in high-concentration NaCl solution. It is found that many peptide conformations cannot exist in equilibrium with the salt-water solvent as a single liquid phase. This suggests a single explanation for salting proteins into and out of solution, unique biologically active protein structures, and small energy differences between denatured and folded states, while also implying a mechanism for the resolution to the Levinthal paradox.

AB - Thermodynamic stability and statistical mechanical theory are applied to a model of a zwitterionic tripeptide of sequence Gly-Ala-Gly in high-concentration NaCl solution. It is found that many peptide conformations cannot exist in equilibrium with the salt-water solvent as a single liquid phase. This suggests a single explanation for salting proteins into and out of solution, unique biologically active protein structures, and small energy differences between denatured and folded states, while also implying a mechanism for the resolution to the Levinthal paradox.

UR - http://www.scopus.com/inward/record.url?scp=33751155223&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33751155223&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:33751155223

VL - 99

SP - 1

EP - 2

JO - Journal of Physical Chemistry

JF - Journal of Physical Chemistry

SN - 0022-3654

IS - 1

ER -