ArticleBiophysical journal2010
Folding network of villin headpiece subdomain.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- Variational embedding of protein folding simulations using Gaussian mixture variational autoencoders.The Journal of chemical physics · 2021Article
- Quantitative Analysis of Protein Unfolded State Energetics: Experimental and Computational Studies Demonstrate That Non-Native Side-Chain Interactions Stabilize Local Native Backbone Structure.The journal of physical chemistry. B · 2021Article
- Heterogeneity in the Folding of Villin Headpiece Subdomain HP36.The journal of physical chemistry. B · 2018Article
- Mechanism of p27 Unfolding for CDK2 Reactivation.Scientific reports · 2016Article
- Characterizing a partially ordered miniprotein through folding molecular dynamics simulations: Comparison with the experimental data.Protein science : a publication of the Protein Society · 2016Article
- A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain.Biophysical journal · 2015Article
- Quantifying the Sources of Kinetic Frustration in Folding Simulations of Small Proteins.Journal of chemical theory and computation · 2014Article
- Ultrafast folding kinetics and cooperativity of villin headpiece in single-molecule force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The protein folding network indicates that the ultrafast folding mutant of villin headpiece subdomain has a deeper folding funnel.The Journal of chemical physics · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Protein folding is a complex multidimensional process that is difficult to illustrate by the traditional analyses based on one- or two-dimensional profiles. Analyses based on transition networks have become an alternative approach that has the potential to reveal detailed features of protein folding dynamics. However, due to the lack of successful reversible folding of proteins from conventional molecular-dynamics simulations, this approach has rarely been utilized. Here, we analyzed the folding network from several 10 μs conventional molecular-dynamics reversible folding trajectories of villin headpiece subdomain (HP35). The folding network revealed more complexity than the traditional two-dimensional map and demonstrated a variety of conformations in the unfolded state, intermediate states, and the native state. Of note, deep enthalpic traps at the unfolded state were observed on the folding landscape. Furthermore, in contrast to the clear separation of the native state and the primary intermediate state shown on the two-dimensional map, the two states were mingled on the folding network, and prevalent interstate transitions were observed between these two states. A more complete picture of the folding mechanism of HP35 emerged when the traditional and network analyses were considered together.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.