Statistical molecular model for hydrated peptides

1 September 1982

journal article
research article
Published by Wiley in International Journal of Peptide and Protein Research

Vol. 20 (3) , 188-193
https://doi.org/10.1111/j.1399-3011.1982.tb03048.x

Abstract

A statistical molecular model for hydrated peptides is used to simulate the behavior of various peptide chains in aqueous solution. The reliability of the model is ascertained by the evolution of the characteristic ratio, Cn, for hydrophobic and hydrophilic polypeptide chains, such as, respectively, poly-Ala and poly-Ser. The comparison of computed and experimental properties related to non radiative energy transfer of angiotensin II analogs, assuming that an ensemble of conformers is a satisfactory representation of the state of these molecules in water, provides further support for the model.

Keywords

This publication has 17 references indexed in Scilit:

Conformational studies of dansylated enkephalins by fluorescence transfer measurements. Proton nuclear magnetic resonance spectroscopy and theoretical calculations
Biochemistry, 1981
HYDRATION OF AMINO ACIDS, PEPTIDES, AND MODEL COMPOUNDS
Annals of the New York Academy of Sciences, 1981
DETERMINATION OF THE AVERAGE END‐TO‐END DISTANCE OF TWO ANGIOTENSIN II ANALOGS BY RESONANCE ENERGY TRANSFER
International Journal of Peptide and Protein Research, 1980
Statistical molecular models for angiotensin II and enkephalin related to NMR coupling constants
The Journal of Physical Chemistry, 1980
Model for the conformational analysis of hydrated peptides. Effect of hydration on the conformational stability of the terminally blocked residues of the 20 naturally occurring amino acids
Biopolymers, 1979
Conformation of naturally-occurring peptides in surfactant solution: Its relation to the structure-forming potential of amino acid sequence
Biochemical and Biophysical Research Communications, 1978
The pH dependence of the conformation of angiotensin peptides by nuclear magnetic resonance: cis-trans isomerism of proline 7
Biochemistry, 1976
Proton magnetic double-resonance study of angiotensin II (Asn¹Val⁵) in aqueous solution employing correlation spectroscopy. Assignment of peptide NH resonances and transfer of saturation from water.
Biochemistry, 1974
Investigation of the Structure of Angiotensin II Using ¹³C Nuclear‐Magnetic‐Resonance Spectra
European Journal of Biochemistry, 1972
Statistical mechanics of chain molecules
Biopolymers, 1969