ArticleBiochemistry2012
Mapping molecular flexibility of proteins with site-directed spin labeling: a case study of myoglobin.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 63 citations in OpenAlex.
- Capturing protein dynamics across timescales with site-directed spin labeling electron paramagnetic resonance spectroscopy.Current opinion in structural biology · 2025Review
- A high-sensitivity stopped-flow EPR system to monitor millisecond conformational kinetics in spin-labeled proteins.Protein science : a publication of the Protein Society · 2025Article
- A pressure-jump EPR system to monitor millisecond conformational exchange rates of spin-labeled proteins.Protein science : a publication of the Protein Society · 2024Article
- A pressure-jump EPR system to monitor millisecond conformational exchange rates of spin-labeled proteins.bioRxiv : the preprint server for biology · 2024Article
- A Highly Ordered Nitroxide Side Chain for Distance Mapping and Monitoring Slow Structural Fluctuations in Proteins.Applied magnetic resonance · 2024Article
- A novel approach to modeling side chain ensembles of the bifunctional spin label RX.bioRxiv : the preprint server for biology · 2023Article
- Transient On- and Off-Pathway Protein Folding Intermediate States Characterized with NMR Relaxation Dispersion.The journal of physical chemistry. B · 2022Article
- DEER Analysis of GPCR Conformational Heterogeneity.Biomolecules · 2021Review
- Deciphering molecular details of the RAC-ribosome interaction by EPR spectroscopy.Scientific reports · 2021Article
- A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone.Journal of molecular biology · 2020Article
- A Global Minimization Toolkit for Batch-Fitting and χBiophysical journal · 2020Article
- Conformational Dynamics in Extended RGD-Containing Peptides.Biomacromolecules · 2020Article
- Paramagnetic NMR in drug discovery.Journal of biomolecular NMR · 2020Review
- 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
- Accessing local structural disruption of Bid protein during thermal denaturation by absorption-mode ESR spectroscopy.RSC advances · 2018Article
- Site-directed spin label electron paramagnetic resonance spectroscopy as a probe of conformational dynamics in the Fe(III) "locked-off" state of the CO-sensing transcription factor CooA.Protein science : a publication of the Protein Society · 2018Article
- Structural basis of siRNA recognition by TRBP double-stranded RNA binding domains.The EMBO journal · 2018Article
- Protonation state of glutamate 73 regulates the formation of a specific dimeric association of mVDAC1.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- EPR Spectroscopy Targets Structural Changes in the E. coli Membrane Fusion CusB upon Cu(I) Binding.Biophysical journal · 2017Article
- Bacterial Chemoreceptor Dynamics: Helical Stability in the Cytoplasmic Domain Varies with Functional Segment and Adaptational Modification.Journal of molecular biology · 2016Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Site-directed spin labeling (SDSL) has potential for mapping protein flexibility under physiological conditions. The purpose of the present study was to explore this potential using 38 singly spin-labeled mutants of myoglobin distributed throughout the sequence. Correlation of the EPR spectra with protein structure provides new evidence that the site-dependent variation in line shape, and hence motion of the spin label, is due largely to differences in mobility of the helical backbone in the ns time range. Fluctuations between conformational substates, typically in the μs-ms time range, are slow on the EPR time scale, and the spectra provide a snapshot of conformational equilibria frozen in time as revealed by multiple components in the spectra. A recent study showed that osmolyte perturbation can positively identify conformational exchange as the origin of multicomponent spectra (López et al. (2009), Protein Sci. 18, 1637). In the present study, this new strategy is employed in combination with line shape analysis and pulsed-EPR interspin distance measurements to investigate the conformation and flexibility of myoglobin in three folded and partially folded states. The regions identified to be in conformational exchange in the three forms agree remarkably well with those assigned by NMR, but the faster time scale of EPR allows characterization of localized states not detected in NMR. Collectively, the results suggest that SDSL-EPR and osmolyte perturbation provide a facile means for mapping the amplitude of fast backbone fluctuations and for detecting sequences in slow conformational exchange in folded and partially folded protein sequences.
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