ArticleProtein science : a publication of the Protein Society2002
Conserved and nonconserved features of the folding pathway of hisactophilin, a beta-trefoil protein.
Article in Protein science : a publication of the Protein Society, 2002. 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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15 citing papers in PubMed, 35 citations in OpenAlex.
- Evolution of a protein folding nucleus.Protein science : a publication of the Protein Society · 2016Article
- Early Folding Events, Local Interactions, and Conservation of Protein Backbone Rigidity.Biophysical journal · 2016Article
- Geometrical Frustration in Interleukin-33 Decouples the Dynamics of the Functional Element from the Folding Transition State Ensemble.PloS one · 2015Article
- Arabidopsis CROLIN1, a novel plant actin-binding protein, functions in cross-linking and stabilizing actin filaments.The Journal of biological chemistry · 2013Article
- Take home lessons from studies of related proteins.Current opinion in structural biology · 2013Review
- Understanding the folding-function tradeoff in proteins.PloS one · 2013Article
- Experimental support for the foldability-function tradeoff hypothesis: segregation of the folding nucleus and functional regions in fibroblast growth factor-1.Protein science : a publication of the Protein Society · 2012Article
- Nonnative interactions regulate folding and switching of myristoylated protein.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family.Glycobiology · 2012Review
- Folding of an all-helical Greek-key protein monitored by quenched-flow hydrogen-deuterium exchange and NMR spectroscopy.European biophysics journal : EBJ · 2012Article
- Energetics and mechanisms of folding and flipping the myristoyl switch in the {beta}-trefoil protein, hisactophilin.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Actin: its cumbersome pilgrimage through cellular compartments.Histochemistry and cell biology · 2008Review
- Multiple routes lead to the native state in the energy landscape of the beta-trefoil family.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Protein folding thermodynamics and dynamics: where physics, chemistry, and biology meet.Chemical reviews · 2006Review
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Based on previous studies of interleukin-1beta (IL-1beta) and both acidic and basic fibroblast growth factors (FGFs), it has been suggested that the folding of beta-trefoil proteins is intrinsically slow and may occur via the formation of essential intermediates. Using optical and NMR-detected quenched-flow hydrogen/deuterium exchange methods, we have measured the folding kinetics of hisactophilin, another beta-trefoil protein that has < 10% sequence identity and unrelated function to IL-1beta and FGFs. We find that hisactophilin can fold rapidly and with apparently two-state kinetics, except under the most stabilizing conditions investigated where there is evidence for formation of a folding intermediate. The hisactophilin intermediate has significant structural similarities to the IL-1beta intermediate that has been observed experimentally and predicted theoretically using a simple, topology-based folding model; however, it appears to be different from the folding intermediate observed experimentally for acidic FGF. For hisactophilin and acidic FGF, intermediates are much less prominent during folding than for IL-1beta. Considering the structures of the different beta-trefoil proteins, it appears that differences in nonconserved loops and hydrophobic interactions may play an important role in differential stabilization of the intermediates for these proteins.
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