Effects of H2O and D2O on polyproline II helical structure

Brian W. Chellgren, Trevor P. Creamer

Research output: Contribution to journalArticlepeer-review

45 Scopus citations

Abstract

The interaction of solvent with a polypeptide chain is one of the primary factors controlling protein folding and stability. In biologically relevant systems, this solvent is most often water. Experimental estimates of the role of water in peptide folding can be obtained from solvent perturbation experiments. The simplest perturbant for H2O water is its isotopic D2O form. The solvation of peptides known to form PII helices with D2O versus H2O increases their propensity to adopt the PII conformation.

Original languageEnglish
Pages (from-to)14734-14735
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number45
DOIs
StatePublished - Nov 17 2004

ASJC Scopus subject areas

  • Catalysis
  • Chemistry (all)
  • Biochemistry
  • Colloid and Surface Chemistry

Fingerprint

Dive into the research topics of 'Effects of H2O and D2O on polyproline II helical structure'. Together they form a unique fingerprint.

Cite this