ArticleScience advances2015
Native proteins trap high-energy transit conformations.
Article in Science advances, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- Volume and compressibility differences between protein conformations revealed by high-pressure NMR.Biophysical journal · 2021Article
- Illuminating the dark conformational space of macrocycles using dominant rotors.Nature chemistry · 2021Article
- A complete Fourier-synthesis-based backbone-conformation-dependent library for proteins.Acta crystallographica. Section D, Structural biology · 2021Article
- Mix-and-inject XFEL crystallography reveals gated conformational dynamics during enzyme catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- RNA folding pathways in stop motion.Nucleic acids research · 2016Article
- Empirical Corrections to the Amber RNA Force Field with Target Metadynamics.Journal of chemical theory and computation · 2016Article
- On the reliability of peptide nonplanarity seen in ultra-high resolution crystal structures.Protein science : a publication of the Protein Society · 2016Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
During protein folding and as part of some conformational changes that regulate protein function, the polypeptide chain must traverse high-energy barriers that separate the commonly adopted low-energy conformations. How distortions in peptide geometry allow these barrier-crossing transitions is a fundamental open question. One such important transition involves the movement of a non-glycine residue between the left side of the Ramachandran plot (that is, ϕ < 0°) and the right side (that is, ϕ > 0°). We report that high-energy conformations with ϕ ~ 0°, normally expected to occur only as fleeting transition states, are stably trapped in certain highly resolved native protein structures and that an analysis of these residues provides a detailed, experimentally derived map of the bond angle distortions taking place along the transition path. This unanticipated information lays to rest any uncertainty about whether such transitions are possible and how they occur, and in doing so lays a firm foundation for theoretical studies to better understand the transitions between basins that have been little studied but are integrally involved in protein folding and function. Also, the context of one such residue shows that even a designed highly stable protein can harbor substantial unfavorable interactions.
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Registered trials
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