ArticleRSC advances2020
The relative stability of trpzip1 and its mutants determined by computation and experiment.
Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Article
- Computational Insights into Membrane Disruption by Cell-Penetrating Peptides.Journal of chemical information and modeling · 2025Article
- Tertiary Plasticity Drives the Efficiency of Enterocin 7B Interactions with Lipid Membranes.The journal of physical chemistry. B · 2024Article
- Tunable CH/π Interactions within a Tryptophan Zipper Motif to Stabilize the Fold of Long β-Hairpin Peptides.ACS chemical biology · 2023Article
- Correlation between chemical denaturation and the unfolding energetics of Acanthamoeba actophorin.Biophysical journal · 2023Article
- Benchmarking Adaptive Steered Molecular Dynamics (ASMD) on CHARMM Force Fields.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022Article
- Implementation of Telescoping Boxes in Adaptive Steered Molecular Dynamics.Journal of chemical theory and computation · 2022Article
- Folding in Place: Design of β-Strap Motifs to Stabilize the Folding of Hairpins with Long Loops.The Journal of organic chemistry · 2021Article
- Energetics and structure of alanine-rich α-helices via adaptive steered molecular dynamics.Biophysical journal · 2021Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Six mutants of the tryptophan zipper peptide trpzip1 have been computationally and experimentally characterized. We determine the varying roles in secondary structure stability of specific residues through a mutation assay. Four of the mutations directly effect the Trp-Trp interactions and two of the mutations target the salt bridge between Glu5 and Lys8. CD spectra and thermal unfolding are used to determine the secondary structure and stability of the mutants compared to the wildtype peptide. Adaptive steered molecular dynamics has been used to obtain the energetics of the unfolding pathways of the mutations. The hydrogen bonding patterns and side-chain interactions over the course of unfolding have also been calculated and compared to wildtype trpzip1. The key finding from this work is the importance of a stabilizing non-native salt bridge pair present in the K8L mutation.
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Registered trials
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