Thermodynamic properties of peptide solutions. Part 6.—The amino acid side-chain contributions to the partial molar volumes and heat capacities of some tripeptides in aqueous solution
- 31 December 1989
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Faraday Transactions
- Vol. 86 (18), 3117-3123
- https://doi.org/10.1039/ft9908603117
Abstract
Limiting partial molar volumes, V0 2, and partial molar heat capacities, C0 p, 2, have been determined for the tripeptides glycyl-L-valylglycine, glycyl-DL-serylglycine and the D and L isomers of glycylleucylglycine in aqueous solution at 298.15 K. These V0 2 and C0 p, 2 results, in conjunction with those for glycylglycylglycine, were used to estimate the contribution of the side chains to the thermodynamic properties. The results obtained are compared with those estimated using V0 2 and C0 p, 2 data for amino acids and dipeptides. The comparison suggests that the tripeptides of sequence glycyl-X-glycine are reasonable models for estimating the contribution to the thermodynamic properties of proteins made by solvent-accessible side chains.This publication has 42 references indexed in Scilit:
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