Multiple phases of protien gels

Masahiko Annaka, Toyoichi Tanaka

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)40-46
Number of pages7
JournalPhysica A: Statistical Mechanics and its Applications
Issue number1-4
Publication statusPublished - Mar 1 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Statistical and Nonlinear Physics
  • Statistics and Probability


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