ArticleThe Journal of biological chemistry2017
Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Investigation of regioselectivity and thermostability of free and immobilized Pleurotus citrinopileatus lipase.Applied microbiology and biotechnology · 2026Article
- Determinants of Tenascin-C and HIV-1 envelope binding and neutralization.Mucosal immunology · 2019Article
- Does iris(in) bring bad news or good news?Eating and weight disorders : EWD · 2018Review
- The Interaction between the Third Type III Domain from Fibronectin and Anastellin Involves β-Strand Exchange.Biochemistry · 2017Article
- Protein unfolding under isometric tension-what force can integrins generate, and can it unfold FNIII domains?Current opinion in structural biology · 2017Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Globular proteins are not permanently folded but spontaneously unfold and refold on time scales that can span orders of magnitude for different proteins. A longstanding debate in the protein-folding field is whether unfolding rates or folding rates correlate to the stability of a protein. In the present study, we have determined the unfolding and folding kinetics of 10 FNIII domains. FNIII domains are one of the most common protein folds and are present in 2% of animal proteins. FNIII domains are ideal for this study because they have an identical seven-strand β-sandwich structure, but they vary widely in sequence and thermodynamic stability. We assayed thermodynamic stability of each domain by equilibrium denaturation in urea. We then assayed the kinetics of domain opening and closing by a technique known as thiol exchange. For this we introduced a buried Cys at the identical location in each FNIII domain and measured the kinetics of labeling with DTNB over a range of urea concentrations. A global fit of the kinetics data gave the kinetics of spontaneous unfolding and refolding in zero urea. We found that the folding rates were relatively similar, ∼0.1-1 s
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Registered trials
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