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Biochemistry. 2006 Dec 12;45(49):14559-66.

An unfolding story of helical transmembrane proteins.

Author information

1
Department of Biology, University of Texas, San Antonio, Texas 78249, USA. Robert.Renthal@UTSA.edu

Abstract

Reversible unfolding of helical transmembrane proteins could provide valuable information about the free energy of interaction between transmembrane helices. Thermal unfolding experiments suggest that this process for integral membrane proteins is irreversible. Chemical unfolding has been accomplished with organic acids, but the unfolding or refolding pathways involve irreversible steps. Sodium dodecyl sulfate (SDS) has been used as a perturbant to study reversible unfolding and refolding kinetics. However, the interpretation of these experiments is not straightforward. It is shown that the results could be explained by SDS binding without substantial unfolding. Furthermore, the SDS-perturbed state is unlikely to include all of the entropy terms involved in an unfolding process. Alternative directions for future research are suggested: fluorinated alcohols in homogeneous solvent systems, inverse micelles, and fragment association studies.

PMID:
17144649
PMCID:
PMC2569854
DOI:
10.1021/bi0620454
[Indexed for MEDLINE]
Free PMC Article

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