Multiple phases of protien gels

Masahiko Annaka and Toyoichi Tanaka

Physica A: Statistical Mechanics and its Applications, 1994, vol. 204, issue 1, 40-46

Abstract: A multiple phase transition was observed in gels made by covalently cross-linking proteins in either native or denatured state. The enzymatic activity of the gels prepared from native α-chymotrypsin was determined for each of the multiple phases. The reversibility of the swelling degrees and the enzymatic reaction rates upon phase transition suggests that the protein is at a free energy minimum and thus in a phase.

Date: 1994
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Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:204:y:1994:i:1:p:40-46

DOI: 10.1016/0378-4371(94)90416-2

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