GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.
The chaperonin GroEL binds folding intermediates of four-disulfidehen lysozyme transiently within its central cavity. Using stopped flow fluorescence we show that GroEL binds early intermediates in folding and accelerates the slow kinetic phase that reflects the reversal of non-native interactions i...
Main Authors: | Coyle, J, Texter, F, Ashcroft, A, Masselos, D, Robinson, C, Radford, SE |
---|---|
Format: | Journal article |
Language: | English |
Published: |
1999
|
Similar Items
-
Structural and mechanistic consequences of polypeptide binding by GroEL.
by: Coyle, J, et al.
Published: (1997) -
Structural and mechanistic consequences of polypeptide binding by GroEL
by: Coyle, J, et al.
Published: (1997) -
A near-native state on the slow refolding pathway of hen lysozyme.
by: Kulkarni, S, et al.
Published: (1999) -
Probing conformations of GroEL-bound substrate proteins by mass spectrometry.
by: Robinson, C, et al.
Published: (1998) -
Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.
by: Robinson, C, et al.
Published: (1994)