ArticleProceedings of the National Academy of Sciences of the United States of America2005
Hairpin folding rates reflect mutations within and remote from the turn region.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Tunable CH/π Interactions within a Tryptophan Zipper Motif to Stabilize the Fold of Long β-Hairpin Peptides.ACS chemical biology · 2023Article
- Modulating the folding and binding of peptides using a stimuli-responsive molecular tweezer.Chemical science · 2023Article
- Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry.Chemical reviews · 2022Review
- Kirkwood-Buff-Derived Force Field for Peptides and Proteins: Applications of KBFF20.Journal of chemical theory and computation · 2021Article
- Accelerating atomistic simulations of proteins using multiscale enhanced sampling with independent tempering.Journal of computational chemistry · 2021Article
- Validation of DBFOLD: An efficient algorithm for computing folding pathways of complex proteins.PLoS computational biology · 2020Article
- Optimization of a β-sheet-cap for long loop closure.Biopolymers · 2017Article
- Aryl-aryl interactions in designed peptide folds: Spectroscopic characteristics and optimal placement for structure stabilization.Biopolymers · 2016Article
- Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.The Journal of chemical physics · 2015Article
- Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes.Angewandte Chemie (International ed. in English) · 2015Review
- An improved capping unit for stabilizing the ends of associated β-strands.FEBS letters · 2014Article
- Folding dynamics and pathways of the trp-cage miniproteins.Biochemistry · 2014Article
- Captides: rigid junctions between beta sheets and small molecules.Journal of peptide science : an official publication of the European Peptide Society · 2014Article
- How quickly can a β-hairpin fold from its transition state?The journal of physical chemistry. B · 2014Article
- Circular permutation of a WW domain: folding still occurs after excising the turn of the folding-nucleating hairpin.Journal of the American Chemical Society · 2014Article
- PRIMO: A Transferable Coarse-grained Force Field for Proteins.Journal of chemical theory and computation · 2013Article
- 13C structuring shifts for the analysis of model β-hairpins and β-sheets in proteins: diagnostic shifts appear only at the cross-strand H-bonded residues.Journal of biomolecular NMR · 2013Article
- Mutational effects on the folding dynamics of a minimized hairpin.Biochemistry · 2013Article
- Further optimization of a hybrid united-atom and coarse-grained force field for folding simulations: Improved backbone hydration and interactions between charged side chains.Journal of chemical theory and computation · 2012Article
- Thermodynamics of protein folding using a modified Wako-Saitô-Muñoz-Eaton model.Journal of biological physics · 2012Article
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Authors and funding
4 authors.
Funding
Abstract
Hairpins play a central role in numerous protein folding and misfolding scenarios. Prior studies of hairpin folding, many conducted with analogs of a sequence from the B1 domain of protein G, suggest that faster folding can be achieved only by optimizing the turn propensity of the reversing loop. Based on studies using dynamic NMR, the native GB1 sequence is a slow folding hairpin (k(F)(278)=1.5 x 10(4)/s). GB1 hairpin analogs spanning a wide range of thermodynamic stabilities (DeltaG(U)(298)=-3.09 to+3.25 kJ/mol) were examined. Fold-stabilizing changes in the reversing loop can act either by accelerating folding or retarding unfolding; we present examples of both types. The introduction of an attractive side-chain/side-chain Coulombic interaction at the chain termini further stabilizes this hairpin. The 1.9-fold increase in folding rate constant observed for this change at the chain termini implies that this Coulombic interaction contributes before or at the transition state. This observation is difficult to rationalize by "zipper" folding pathways that require native turn formation as the sole nucleating event; it also suggests that Coulombic interactions should be considered in the design of systems intended to probe the protein folding speed limit.
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