The folding-unfolding transition of equine lysozyme
β Scribed by P. Haezebrouck; H. Van Dael
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 238 KB
- Volume
- 294
- Category
- Article
- ISSN
- 0022-2860
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π SIMILAR VOLUMES
The influence of proline cis-trans isomerization on the kinetics of lysozyme unfolding was examined carefully according to the theory of Hagerman and Baldwin "1976) Biochemistry 15, 1462-14731. As a result, the kinetics of lysozyme unfolding was found to follow the two-state transition model well. T
The reversible refolding of a lysozyme derivative containing an extra crosslink between Glu 35 and Trp 108 was observed at pH 3.7 in solutions of 4.5M LiBr and 4.6M 1-PrOH. The rate constants of unfolding and folding for crosslinked lysozyme were compared with those for intact lysozyme. In LiBr solu
## Abstract A threeβdimensional lattice model of protein designed to assimilate lysozyme is introduced. An attractive interaction is assumed to work between preassigned specific pairs of units, when they occupy the nearestβnighbor lattice points. The behavior of this lattice lysozyme is studied by