ArticleProceedings of the National Academy of Sciences of the United States of America2008
Barrierless evolution of structure during the submillisecond refolding reaction of a small protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 31 citations in OpenAlex.
- Assessing Site-Specific Enhancements Imparted by Hyperpolarized Water in Folded and Unfolded Proteins by 2D HMQC NMR.Journal of the American Chemical Society · 2020Article
- How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016Review
- Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation.Journal of the American Chemical Society · 2015Article
- Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state.Biophysical journal · 2013Article
- Structural and dynamic aspects of protein clocks: how can they be so slow and stable?Cellular and molecular life sciences : CMLS · 2012Review
- The origin of nonmonotonic complex behavior and the effects of nonnative interactions on the diffusive properties of protein folding.Biophysical journal · 2010Article
- Direct evidence for a dry molten globule intermediate during the unfolding of a small protein.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Continuous dissolution of structure during the unfolding of a small protein.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Ruggedness in the folding landscape of protein L.HFSP journal · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To determine whether a protein folding reaction can occur in the absence of a dominant barrier is crucial for understanding its complexity. Here direct ultrafast kinetic measurements have been used to study the initial submillisecond (sub-ms) folding reaction of the small protein barstar. The cooperativity of the initial folding reaction has been explored by using two probes: fluorescence resonance energy transfer, through which the contraction of two intramolecular distances is measured, and the binding of 8-anilino-1-naphthalene sulfonic acid, through which the formation of hydrophobic clusters is monitored. A fast chain contraction is shown to precede the formation of hydrophobic clusters, indicating that the sub-ms folding reaction is not cooperative. The observed rate constant of the sub-ms folding reaction monitored by 8-anilino-1-naphthalene sulfonic acid fluorescence has been found to be the same in stabilizing conditions (low urea concentrations), in which specific structure is formed, and in marginally stabilizing conditions (higher urea concentrations), where virtually no structure is formed in the product of the sub-ms folding reaction. The observation that the folding rate is independent of the folding conditions suggests that the initial folding reaction occurs in the absence of a dominant free energy barrier. These results provide kinetic evidence that the formation of specific structure need not be slowed down by any significant free energy barrier during the course of a very fast protein folding reaction.
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