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Partial molar heat capacities of the side chains of some amino acid residues in aqueous solution. The influence of the neighboring charges.

作者信息

Makhatadze G I, Gill S J, Privalov P L

机构信息

Institute of Protein Research, Academy of Sciences of the U.S.S.R., Pushchino, Moscow Region 142292, U.S.S.R.

出版信息

Biophys Chem. 1990 Oct;38(1-2):33-7. doi: 10.1016/0301-4622(90)80037-8.

Abstract

Partial molar heat capacities of the side chains of some amino acid residues (Ala, Val, Leu, Ile, Ser) have been determined over a broad temperature range from calorimetric heat capacity measurements of the corresponding tripeptides and cyclodipeptides. The data obtained are compared with those determined earlier from the heat capacities of analog compounds. It is shown that in amino acids and even tripeptides of the Gly-X-Gly type, the influence of the end charges on the heat capacity of the side chain is rather significant even in buffered solutions of high ionic strength.

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