Protein folding transition states probed by loop extension

We propose a new way to characterize protein folding transition states by (1) insertion of one or more residues into an unstructured protein loop, (2) measurement of the effect on protein folding kinetics and thermodynamics, and (3) analysis of the results in terms of a rate‐equilibrium free energy...

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Bibliographic Details
Published in:Protein science 2008-01, Vol.17 (1), p.183-186
Main Author: Sanchez, Ignacio Enrique
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
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Kinetics
loop
Protein Folding
Proteins - chemistry
Proteins - metabolism
rate‐equilibrium free energy relationships
Thermodynamics
transition state
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Summary:We propose a new way to characterize protein folding transition states by (1) insertion of one or more residues into an unstructured protein loop, (2) measurement of the effect on protein folding kinetics and thermodynamics, and (3) analysis of the results in terms of a rate‐equilibrium free energy relationship, αLoop. αLoop reports on the fraction of molecules that form the perturbed loop in the transition state. Interpretation of the changes in equilibrium free energy using standard polymer theory can help detect residual structure in the unfolded state. We illustrate our approach with data for the model proteins CI2 and the alpha spectrin SH3 domain.
ISSN:0961-8368
1469-896X
DOI:10.1110/ps.073217708