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.
|Number of pages||7|
|Journal||Physica A: Statistical Mechanics and its Applications|
|Publication status||Published - Mar 1 1994|
All Science Journal Classification (ASJC) codes
- Statistics and Probability
- Condensed Matter Physics