ArticleBiochemistry2013
Mutational effects on the folding dynamics of a minimized hairpin.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Structure-Based Experimental Datasets for Benchmarking Protein Simulation Force Fields [Article v1.0].Living journal of computational molecular science · 2025Article
- Atomistic simulations reveal impacts of missense mutations on the structure and function of SynGAP1.Briefings in bioinformatics · 2024Article
- Folding in Place: Design of β-Strap Motifs to Stabilize the Folding of Hairpins with Long Loops.The Journal of organic chemistry · 2021Article
- 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
- Long range Trp-Trp interaction initiates the folding pathway of a pro-angiogenic β-hairpin peptide.Scientific reports · 2015Article
- 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
- Intermediates in the folding equilibrium of repeat proteins from the TPR family.European biophysics journal : EBJ · 2014Article
- Captides: rigid junctions between beta sheets and small molecules.Journal of peptide science : an official publication of the European Peptide Society · 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
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5 authors.
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Abstract
The fold stabilities and folding dynamics of a series of mutants of a model hairpin, KTW-NPATGK-WTE (HP7), are reported. The parent system and the corresponding DPATGK loop species display submicrosecond folding time constants. The mutational studies revealed that ultrafast folding requires both some prestructuring of the loop and a favorable interaction between the chain termini in the transition state. In the case of YY-DPETGT-WY, another submicrosecond folding species [Davis, C. M., Xiao, S., Raleigh, D. P., and Dyer, R. B. (2012) J. Am. Chem. Soc. 134, 14476-14482], a hydrophobic cluster provides the latter. In the case of HP7, the Coulombic interaction between the terminal NH3(+) and CO2(-) units provides this; a C-terminal Glu to amidated Ala mutation results in a 5-fold retardation of the folding rate. The effects of mutations within the reversing loop indicate the balance between loop flexibility (favoring fast conformational searching) and turn formation in the unfolded state is a major factor in determining the folding dynamics. The -NAAAKX- loops examined display no detectable turn formation propensity in other hairpin constructs but do result in stable analogues of HP7. Peptide KTW-NAAAKK-WTE displays the same fold stability as HP7, but both the folding and unfolding time constants are greater by a factor of 20.
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