ArticleBiophysical reviews2010
Protein structural dynamics revealed by site-directed spin labeling and multifrequency EPR.
Article in Biophysical reviews, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed.
- Allosteric Modulation of SERCA Pumps in Health and Disease: Structural Dynamics, Posttranslational Modifications, and Therapeutic Potential.Journal of molecular biology · 2025Review
- Human CEACAM1 N-domain dimerization is independent from glycan modifications.Structure (London, England : 1993) · 2022Article
- Characterization of protein unfolding by fast cross-linking mass spectrometry using di-ortho-phthalaldehyde cross-linkers.Nature communications · 2022Article
- Conformational Dynamics in Extended RGD-Containing Peptides.Biomacromolecules · 2020Article
- Quantifying residue-specific conformational dynamics of a highly reactive 29-mer peptide.Scientific reports · 2020Article
- Structural and dynamic origins of ESR lineshapes in spin-labeled GB1 domain: the insights from spin dynamics simulations based on long MD trajectories.Scientific reports · 2020Article
- ESR as a monitoring method of the interactions between TEMPO-functionalized magnetic nanoparticles and yeast cells.Scientific reports · 2019Article
- Myosin lever arm orientation in muscle determined with high angular resolution using bifunctional spin labels.The Journal of general physiology · 2019Article
- Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Site-Specific Internal Motions in GB1 Protein Microcrystals Revealed by 3D ²H-¹³C-¹³C Solid-State NMR Spectroscopy.Journal of the American Chemical Society · 2016Article
- EPR Studies of Gating Mechanisms in Ion Channels.Methods in enzymology · 2015Review
- Electron paramagnetic resonance spectroscopy of nitroxide-labeled calmodulin.The protein journal · 2014Article
- Technological advances in site-directed spin labeling of proteins.Current opinion in structural biology · 2013Review
- Structure and dynamics of an imidazoline nitroxide side chain with strongly hindered internal motion in proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
- Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Multifrequency electron paramagnetic resonance (EPR), combined with site-directed spin labeling, is a powerful spectroscopic tool to characterize protein dynamics. The lineshape of an EPR spectrum reflects combined rotational dynamics of the spin probe's local motion within a protein, reorientations of protein domains, and overall protein tumbling. All these motions can be restricted and anisotropic, and separation of these motions is important for thorough characterization of protein dynamics. Multifrequency EPR distinguishes between different motions of a spin-labeled protein, due to the frequency dependence of EPR resolution to fast and slow motion of a spin probe. This gives multifrequency EPR its unique capability to characterize protein dynamics in great detail. In this review, we analyze what makes multifrequency EPR sensitive to different rates of spin probe motion and discuss several examples of its usage to separate spin probe dynamics and overall protein dynamics, to characterize protein backbone dynamics, and to resolve protein conformational states.
Identifiers
What OpenQuestion holds
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.