ISSN:
1435-1536
Keywords:
PEG
;
amino acid
;
excess volume
;
excess compressibility
;
hydrophobic interaction
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
,
Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
Notes:
Abstract The volume and compressibility changes on mixing aqueous solutions of the amino acid and poly(ethylene glycol) were measured with a vibration densimeter and a sing-around velocimeter at 298.15 K. For the system of alanine-PEG-H2O, the additivity rule for the mean apparent molal volume and compressibility at infinite dilution held, and the excess volume and compressibility changes on mixing were obtained. For the system of glycine-PEG-H2O, the additivity rule for the mean apparent molal compressibility at infinite dilution did not hold. While the mean apparent molal volume and compressibility changes were negative and positive for the systems of another amino acid-PEG-H2O, respectively, where amino acids were valine, isoleucine, leucine, phenylalanine, and tryptophan. These results suggest that glycine and alanine are excluded from the hydration layer around PEG chain and the amino acids with a larger side chain than alanine are bound to the PEG chain due to the hydrophobic interaction. The hydration number per monomer around PEG chain was estimated to be 3.9.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00659449
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