ArticleThe journal of physical chemistry letters2012
Exposing the Moving Parts of Proteins with NMR Spectroscopy.
Article in The journal of physical chemistry letters, 2012. 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.
- The hairpin extension controls solvent access to the chromophore binding pocket in a bacterial phytochrome: a UV-vis absorption spectroscopy study.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021Article
- NMR Relaxation Dispersion Reveals Macrocycle Breathing Dynamics in a Cyclodextrin-based Rotaxane.Journal of the American Chemical Society · 2020Article
- Direct observation of dynamic protein interactions involving human microtubules using solid-state NMR spectroscopy.Nature communications · 2020Article
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Deriving quantitative dynamics information for proteins and RNAs using ROTDIF with a graphical user interface.Journal of biomolecular NMR · 2013Article
- Revealing the properties of plant defensins through dynamics.Molecules (Basel, Switzerland) · 2013Review
- The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation.Current opinion in structural biology · 2013Review
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for investigating the dynamics of biomolecules since it provides a description of motion that is comprehensive, site-specific, and relatively non-invasive. In particular, the study of protein dynamics has benefited from sustained methodological advances in NMR that have expanded the scope and time scales of accessible motion. Yet, many of these advances may not be well known to the more general physical chemistry community. Accordingly, this Perspective provides a glimpse of some of the more powerful methods in liquid state NMR that are helping reshape our understanding of functional motions of proteins.
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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.