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.
Original language | English (US) |
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Pages (from-to) | 15065-15068 |
Number of pages | 4 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 102 |
Issue number | 42 |
DOIs | |
State | Published - Oct 18 2005 |
Keywords
- Group transfer free energies
- Transfer model
- m value
ASJC Scopus subject areas
- General