Predicting the energetics of osmolyte-induced protein folding/unfolding

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چکیده

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Predicting the energetics of osmolyte-induced protein folding/unfolding.

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 prot...

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A molecular mechanism for osmolyte-induced protein stability.

Osmolytes are small organic compounds that affect protein stability and are ubiquitous in living systems. In the equilibrium protein folding reaction, unfolded (U) native (N), protecting osmolytes push the equilibrium toward N, whereas denaturing osmolytes push the equilibrium toward U. As yet, there is no universal molecular theory that can explain the mechanism by which osmolytes interact wit...

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Sequence-specific interactions between proteins and DNA play a central role in DNA replication, repair, recombination, and control of gene expression. These interactions can be studied in vitro using microfluidics, protein-binding microarrays (PBMs), and other high-throughput techniques. Here we develop a biophysical approach to predicting protein-DNA binding specificities from high-throughput ...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2005

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.0507053102