ArticleProceedings of the National Academy of Sciences of the United States of America1999
Transition state heterogeneity in GCN4 coiled coil folding studied by using multisite mutations and crosslinking.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed.
- The transition state for coupled folding and binding of a disordered DNA binding domain resembles the unbound state.Nucleic acids research · 2024Article
- Engineered Metal-Binding Sites to Probe Protein Folding Transition States: Psi Analysis.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly.Biophysical journal · 2020Article
- Stability, folding dynamics, and long-range conformational transition of the synaptic t-SNARE complex.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Cooperative folding near the downhill limit determined with amino acid resolution by hydrogen exchange.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Even with nonnative interactions, the updated folding transition states of the homologs Proteins G & L are extensive and similar.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Tightening up the structure, lighting up the pathway: Application of molecular constraints and light to manipulate protein folding, self-assembly and function.Science China. Chemistry · 2014Article
- Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Sequence-resolved free energy profiles of stress-bearing vimentin intermediate filaments.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Hierarchical cascades of instability govern the mechanics of coiled coils: helix unfolding precedes coil unzipping.Biophysical journal · 2014Article
- How quickly can a β-hairpin fold from its transition state?The journal of physical chemistry. B · 2014Article
- Is Five Percent Too Small? Analysis of the Overlaps between Disorder, Coiled Coil and Collagen Predictions in Complete Proteomes.Proteomes · 2014Article
- Unique features of the anti-parallel, heterodimeric coiled-coil interaction between methyl-cytosine binding domain 2 (MBD2) homologues and GATA zinc finger domain containing 2A (GATAD2A/p66α).The Journal of biological chemistry · 2013Article
- A "Link-Psi" strategy using crosslinking indicates that the folding transition state of ubiquitin is not very malleable.Protein science : a publication of the Protein Society · 2012Article
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- Structured pathway across the transition state for peptide folding revealed by molecular dynamics simulations.PLoS computational biology · 2011Article
- Highly anisotropic stability and folding kinetics of a single coiled coil protein under mechanical tension.Journal of the American Chemical Society · 2011Article
- The folding of single domain proteins--have we reached a consensus?Current opinion in structural biology · 2011Review
- The effects of pK(a) tuning on the thermodynamics and kinetics of folding: design of a solvent-shielded carboxylate pair at the a-position of a coiled-coil.Biophysical journal · 2010Article
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5 authors.
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Abstract
We have investigated the folding behavior of dimeric and covalently crosslinked versions of the 33-residue alpha-helical GCN4-p1 coiled coil derived from the leucine zipper region of the transcriptional activator GCN4. The effects of multisite substitutions indicate that folding occurs along multiple routes with nucleation sites located throughout the protein. The similarity in activation energies of the different routes together with an analysis of intrinsic helical propensities indicate that minimal helix is present before a productive collision of the two chains. However, approximately one-third to one-half of the total helical structure is formed in the postcollision transition state ensemble. For the crosslinked, monomeric version, folding occurs along a single robust pathway. Here, the region nearest the crosslink, with the least helical propensity, is structured in the transition state whereas the region farthest from the tether, with the most propensity, is completely unstructured. Hence, the existence of transition state heterogeneity and the selection of folding routes critically depend on chain topology.
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