Thermodynamic properties of peptide solutions. Part 11. Partial molar isentropic pressure coefficients in aqueous solutions of some tripeptides that model protein side-chains
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,Biophysics
Reference26 articles.
1. Solvation of amino acid residues in water and urea-water mixtures: Volumes and heat capacities of 20 amino acids in water and in 8 molar urea at 25�C
2. Solid model compounds and the thermodynamics of protein unfolding
3. Heat capacity of proteins
4. Partial molar volumes of the amino acid side-chains of proteins in aqueous solution: Some comments on their estimation using partial molar volumes of amino acids and small peptides
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1. Thermodynamic properties of peptide solutions 20. Partial molar volumes and isothermal compressions for some tripeptides of sequence gly-X-gly (X = gly, ala, leu, asn, thr, and tyr) in aqueous solution at T = 298.15 K and p = (10–120) MPa;The Journal of Chemical Thermodynamics;2016-08
2. Volumetric, acoustic and viscometric behaviour of dipotassium hydrogen phosphate and disodium hydrogen phosphate in aqueous solution of N-acetyl glycine at different temperatures;The Journal of Chemical Thermodynamics;2016-03
3. Surfactant–Amino Acid and Surfactant–Surfactant Interactions in Aqueous Medium: a Review;Applied Biochemistry and Biotechnology;2015-07-10
4. Partial molar volumes and compressibilities of glycine betaine in aqueous NaCl solutions at temperatures T=(288.15–318.15)K;Fluid Phase Equilibria;2014-08
5. Group-contribution to limiting partial molar isentropic compressions of small amphiphile molecules in water. The temperature effect;The Journal of Chemical Thermodynamics;2014-02
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