Literature DB >> 17056435

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

G I Makhatadze1, S J Gill, P L Privalov.   

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.

Entities:  

Year:  1990        PMID: 17056435     DOI: 10.1016/0301-4622(90)80037-8

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  2 in total

1.  A molecular framework for temperature-dependent gating of ion channels.

Authors:  Sandipan Chowdhury; Brian W Jarecki; Baron Chanda
Journal:  Cell       Date:  2014-08-21       Impact factor: 41.582

2.  Thermodynamic prediction of glycine polymerization as a function of temperature and pH consistent with experimentally obtained results.

Authors:  Norio Kitadai
Journal:  J Mol Evol       Date:  2014-03-21       Impact factor: 2.395

  2 in total

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