Journal
ANNUAL REVIEW OF BIOPHYSICS, VOL 43
Volume 43, Issue -, Pages 233-255Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biophys-051013-022926
Keywords
thermodynamics; protein-lipid interactions
Categories
Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM079440] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM079440, R01 GM 07990] Funding Source: Medline
Ask authors/readers for more resources
Fundamental to the central goals of structural biology is knowledge of the energetics of molecular interactions. Because membrane proteins reside in a free energy minimum dictated by their sequences, their lipid environment, and water, one must understand the energetics of membrane protein folding to generate physical descriptions of cellular processes. Several technical obstacles have recently been overcome to enable folding measurements for membrane proteins in lipid and detergent micelle environments, and several new folding free energies have been published within the past ten years. This review discusses the challenges, successes, and novel insights into the physical basis underlying membrane protein folds.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available