ArticleBiochemistry2006
Hydration of the folding transition state ensemble of a protein.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Theoretical Study of the Influence of K20N Glycosylation on the Dynamic Behavior of Im7 Protein.Molecules (Basel, Switzerland) · 2025Article
- Lessons from pressure denaturation of proteins.Journal of the Royal Society, Interface · 2018Review
- Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology.Methods (San Diego, Calif.) · 2018Article
- Application of conventional molecular dynamics simulation in evaluating the stability of apomyoglobin in urea solution.Scientific reports · 2017Article
- Water Determines the Structure and Dynamics of Proteins.Chemical reviews · 2016Review
- Analysis of the size dependence of macromolecular crowding shows that smaller is better.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Interplay between drying and stability of a TIM barrel protein: a combined simulation-experimental study.Journal of the American Chemical Society · 2013Article
- Size and sequence and the volume change of protein folding.Journal of the American Chemical Society · 2011Article
- Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH.Proteins · 2011Article
- High-pressure SAXS study of folded and unfolded ensembles of proteins.Biophysical journal · 2010Article
- Article
- Unique features of the folding landscape of a repeat protein revealed by pressure perturbation.Biophysical journal · 2010Article
- Desolvation and development of specific hydrophobic core packing during Im7 folding.Journal of molecular biology · 2010Article
- Minimizing frustration by folding in an aqueous environment.Archives of biochemistry and biophysics · 2008Article
- Calcium ion-induced stabilization and refolding of agkisacutacin from Agkistrodon acutus venom studied by fluorescent spectroscopy.Journal of fluorescence · 2007Article
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5 authors.
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Abstract
A complete description of the mechanisms of protein folding requires knowledge of the structural and physical character of the folding transition state ensembles (TSEs). A key question concerning the role of hydration of the hydrophobic core in determining folding mechanisms remains. To address this, we probed the state of hydration of the TSE of staphylococcal nuclease (SNase) by examining the fluorescence-detected pressure-jump relaxation behavior of six SNase variants in which a residue in the hydrophobic core, Val-66, was replaced with polar or ionizable residues (Lys, Arg, His, Asp, Glu, and Asn). Because of a large positive activation volume for folding, the major effect of pressure on the wild-type protein is to decrease the folding rate. By the time wild-type SNase reaches the folding transition state, most water has already been expelled from its hydrophobic core. In contrast, the major effect of pressure on the variant proteins is an increase in the unfolding rate due to a large negative activation volume for unfolding. This results from a significant increase in the level of hydration of the TSE when an internal ionizable group is present. These data confirm that the role of water in the folding reaction can differ from protein to protein and that even a single substitution in a critical position can modulate significantly the properties of the TSE.
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