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...
Main Authors: | Texter, F, Coyle, J, Kulkarni, S, Robinson, C, Radford, SE |
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פורמט: | Journal article |
שפה: | English |
יצא לאור: |
1997
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פריטים דומים
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GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.
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Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme.
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The origin of the alpha-domain intermediate in the folding of hen lysozyme.
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Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme.
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יצא לאור: (2000) -
Effect of pH on Diclofenac–Lysozyme Interaction: Structural and Functional Aspect
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