ArticleScience advances2016
Determination of functional collective motions in a protein at atomic resolution using coherent neutron scattering.
Article in Science advances, 2016. 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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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, 40 citations in OpenAlex.
- Extended Sampling of Macromolecular Conformations from Uniformly Distributed Points on Multidimensional Normal Mode Hyperspheres.Journal of chemical theory and computation · 2024Article
- Article
- Controlling the Substrate Specificity of an Enzyme through Structural Flexibility by Varying the Salt-Bridge Density.Molecules (Basel, Switzerland) · 2021Article
- Dynamics of proteins with different molecular structures under solution condition.Scientific reports · 2020Article
- Structural Relaxation Processes and Collective Dynamics of Water in Biomolecular Environments.The journal of physical chemistry. B · 2019Article
- Entropic contribution to enhanced thermal stability in the thermostable P450 CYP119.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Dynamics of water bound to crystalline cellulose.Scientific reports · 2017Article
- `Atomic resolution': a badly abused term in structural biology.Acta crystallographica. Section D, Structural biology · 2017Article
- Thermal activation of 'allosteric-like' large-scale motions in a eukaryotic Lactate Dehydrogenase.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein function often depends on global, collective internal motions. However, the simultaneous quantitative experimental determination of the forms, amplitudes, and time scales of these motions has remained elusive. We demonstrate that a complete description of these large-scale dynamic modes can be obtained using coherent neutron-scattering experiments on perdeuterated samples. With this approach, a microscopic relationship between the structure, dynamics, and function in a protein, cytochrome P450cam, is established. The approach developed here should be of general applicability to protein systems.
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Registered trials
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