Work

Predicting the energetics of osmolyte-induced protein folding/unfolding

Year: 2005

Type: article

Abstract: A primary thermodynamic goal in protein biochemistry is to attain predictive understanding of the detailed energetic changes that are responsible for folding/unfolding. Through use of recently determined free energies of side-chain and backbone transfer from water to osmolytes and Tanford's transfer model, we demonstrate that the long-sought goal of predicting solvent-dependent cooperative protein folding/unfolding free-energy changes (m values) can be achieved. Moreover, the approach permits dissection of the folding/unfolding free-energy changes into individual contributions from the peptide backbone and residue side chains.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.0507053102

Authors: Matthew Auton, D. Wayne Bolen

Institution: The University of Texas Medical Branch at Galveston

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Award: Impact of naturally occurring osmolytes on protein structure and energetics