Abolition of the fast track of lysozyme folding at neutral pH
Studies in this laboratory have shown nat [he reLozolng of lysozyme is accelerated in the presence of equimolar GroEL. We are now investigating the molecular origin of this rate enchancement. The conditions under which the rate enhancement occurs are pH 7.2, 400 mM KCI, and GroEL. The first step in...
المؤلفون الرئيسيون: | Texter, F, Coyle, J, Kulkarni, S, Robinson, C, Radford, SE |
---|---|
التنسيق: | Journal article |
اللغة: | English |
منشور في: |
1997
|
مواد مشابهة
-
GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.
حسب: Coyle, J, وآخرون
منشور في: (1999) -
Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme.
حسب: Eyles, S, وآخرون
منشور في: (1994) -
The origin of the alpha-domain intermediate in the folding of hen lysozyme.
حسب: Matagne, A, وآخرون
منشور في: (1998) -
Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme.
حسب: Matagne, A, وآخرون
منشور في: (2000) -
Effect of pH on Diclofenac–Lysozyme Interaction: Structural and Functional Aspect
حسب: Mohd Basheeruddin, وآخرون
منشور في: (2022-07-01)