Effects of H2O and D2O on Polyproline II Helical Structure
- 26 October 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 126 (45) , 14734-14735
- https://doi.org/10.1021/ja045425q
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.Keywords
This publication has 14 references indexed in Scilit:
- Influence of proline residues on protein conformationPublished by Elsevier ,2004
- Short Sequences of Non-Proline Residues Can Adopt the Polyproline II Helical ConformationBiochemistry, 2004
- Unfolded state of polyalanine is a segmented polyproline II helixProteins-Structure Function and Bioinformatics, 2004
- Polyproline II helix is the preferred conformation for unfolded polyalanine in waterProteins-Structure Function and Bioinformatics, 2004
- Role of Solvent in Determining Conformational Preferences of Alanine Dipeptide in WaterJournal of the American Chemical Society, 2004
- Stable Conformations of Tripeptides in Aqueous Solution Studied by UV Circular Dichroism SpectroscopyJournal of the American Chemical Society, 2003
- A simple model for polyproline II structure in unfolded states of alanine‐based peptidesProtein Science, 2002
- A survey of left‐handed polyproline II helicesProtein Science, 1999
- A study of the structure of water and its dependence on solutes, based on the isotope effects on solvation thermodynamics in waterThe Journal of Chemical Physics, 1985
- Derivative spectroscopy applied to tyrosyl chromophores. Ribonuclease, lima bean inhibitors, insulin, and pancreatic trypsin inhibitorBiochemistry, 1973