Mechanisms of protein folding

The strong correlation between protein folding rates and the contact order suggests that folding rates are largely determined by the topology of the native structure. However, for a given topology, there may be several possible low free energy paths to the native state and the path that is chosen (t...

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Bibliographic Details
Published in:Current Opinion in Structural Biology 2001-02, Vol.11 (1), p.70-82
Main Authors: Grantcharova, Viara, Alm, Eric J, Baker, David, Horwich, Arthur L
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
chaperonin
Chaperonins
contact order
DNA Mutational Analysis
folding transition state
GroEL
GroES
hydrophobicity
kinetic traps
Kinetics
Models, Chemical
Models, Molecular
Protein Binding
Protein Denaturation
Protein Folding
protein structure
Thermodynamics
unfolding
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Summary:The strong correlation between protein folding rates and the contact order suggests that folding rates are largely determined by the topology of the native structure. However, for a given topology, there may be several possible low free energy paths to the native state and the path that is chosen (the lowest free energy path) may depend on differences in interaction energies and local free energies of ordering in different parts of the structure. For larger proteins whose folding is assisted by chaperones, such as the Escherichia coli chaperonin GroEL, advances have been made in understanding both the aspects of an unfolded protein that GroEL recognizes and the mode of binding to the chaperonin. The possibility that GroEL can remove non-native proteins from kinetic traps by unfolding them either during polypeptide binding to the chaperonin or during the subsequent ATP-dependent formation of folding-active complexes with the co-chaperonin GroES has also been explored.
ISSN:0959-440X
1879-033X
DOI:10.1016/S0959-440X(00)00176-7