Articles | Volume 1, issue 2
https://doi.org/10.5194/mr-1-209-2020
© Author(s) 2020. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
https://doi.org/10.5194/mr-1-209-2020
© Author(s) 2020. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
DeerLab: a comprehensive software package for analyzing dipolar electron paramagnetic resonance spectroscopy data
Luis Fábregas Ibáñez
Laboratory of Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, 8093 Zurich, Switzerland
Gunnar Jeschke
Laboratory of Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, 8093 Zurich, Switzerland
Department of Chemistry, University of Washington, Seattle, WA 98195, USA
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Cited
89 citations as recorded by crossref.
- Trendbericht: Elektronen‐Paramagnetische‐Resonanzspektroskopie O. Schiemann 10.1002/nadc.20214106853
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- Modeling of Cu(ii)-based protein spin labels using rotamer libraries Z. Hasanbasri et al. 10.1039/D3CP05951K
- Deconvoluting Monomer- and Dimer-Specific Distance Distributions between Spin Labels in a Monomer/Dimer Mixture Using T1-Edited DEER EPR Spectroscopy T. Schmidt et al. 10.1021/jacs.4c03916
- PDSFit: PDS data analysis in the presence of orientation selectivity, g‐anisotropy, and exchange coupling D. Abdullin et al. 10.1002/mrc.5415
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- Confidence limits in pulse dipolar EPR spectroscopy: estimates for individual measurements V. Syryamina et al. 10.1039/D3CP05797F
- An optimal acquisition scheme for Q-band EPR distance measurements using Cu2+-based protein labels X. Bogetti et al. 10.1039/D2CP01032A
- Design of stimulus-responsive two-state hinge proteins F. Praetorius et al. 10.1126/science.adg7731
- Quantifying methyl tunneling induced (de)coherence of nitroxides in glassy ortho-terphenyl at low temperatures A. Eggeling et al. 10.1039/D3CP01299A
- Ensemble structure of the N-terminal domain (1–267) of FUS in a biomolecular condensate L. Esteban-Hofer et al. 10.1016/j.bpj.2024.01.023
- Methodology for rigorous modeling of protein conformational changes by Rosetta using DEER distance restraints D. del Alamo et al. 10.1371/journal.pcbi.1009107
- Cross-validation of distance measurements in proteins by PELDOR/DEER and single-molecule FRET M. Peter et al. 10.1038/s41467-022-31945-6
- Membrane potential accelerates sugar uptake by stabilizing the outward facing conformation of the Na/glucose symporter vSGLT F. Khan et al. 10.1038/s41467-023-43119-z
- Entschlüsselung der ligandeninduzierten Verdrehung eines homodimeren Enzyms mit Hilfe der gepulsten Elektron‐Elektron‐Doppelresonanz‐Spektroskopie D. Nguyen et al. 10.1002/ange.202108179
- Insights into the Conformational Plasticity of the Protein Kinase Akt1 by Multi‐Lateral Dipolar Spectroscopy J. Stehle et al. 10.1002/chem.202203959
- Enhanced sensitivity for pulse dipolar EPR spectroscopy using variable-time RIDME J. Wort et al. 10.1016/j.jmr.2023.107460
- Pulsed EPR Methods in the Angstrom to Nanometre Scale Shed Light on the Conformational Flexibility of a Fluoride Riboswitch L. Remmel et al. 10.1002/anie.202411241
- Electron paramagnetic resonance spectroscopy in structural-dynamic studies of large protein complexes L. Galazzo & E. Bordignon 10.1016/j.pnmrs.2022.11.001
- Dipolar pathways in dipolar EPR spectroscopy L. Fábregas-Ibáñez et al. 10.1039/D1CP03305K
- Protein delivery to living cells by thermal stimulation for biophysical investigation F. Torricella et al. 10.1038/s41598-022-21103-9
- In situ distance measurements in a membrane transporter using maleimide functionalized orthogonal spin labels and 5-pulse electron-electron double resonance spectroscopy S. Ketter et al. 10.1016/j.jmro.2022.100041
- Measuring conformational equilibria in allosteric proteins with time-resolved tmFRET W. Zagotta et al. 10.1016/j.bpj.2024.01.033
- Dynamic basis of lipopolysaccharide export by LptB2FGC M. Dajka et al. 10.7554/eLife.99338.3
- Zeitaufgelöste Mn2+−NO‐ und NO−NO‐Abstandsmessungen zeigen regulierende Funktion der katalytischen Asymmetrie auf den alternierenden Zugang in einem ABC‐Transporter** M. Rudolph et al. 10.1002/ange.202307091
- Unraveling a Ligand‐Induced Twist of a Homodimeric Enzyme by Pulsed Electron–Electron Double Resonance D. Nguyen et al. 10.1002/anie.202108179
- Exploring tunneling ESEEM beyond methyl groups in nitroxides at low temperatures A. Eggeling et al. 10.1039/D4CP01212G
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- Protein functional dynamics from the rigorous global analysis of DEER data: Conditions, components, and conformations E. Hustedt et al. 10.1085/jgp.201711954
- Dipolar pathways in multi-spin and multi-dimensional dipolar EPR spectroscopy L. Fábregas-Ibáñez et al. 10.1039/D2CP03048A
- EPR spectroscopic characterisation of native CuII-binding sites in human serum albumin K. Ackermann et al. 10.1039/D4DT00892H
- Enzymatic Spin-Labeling of Protein N- and C-Termini for Electron Paramagnetic Resonance Spectroscopy R. Dunleavy et al. 10.1021/acs.bioconjchem.3c00029
- Exploring protein structural ensembles: Integration of sparse experimental data from electron paramagnetic resonance spectroscopy with molecular modeling methods J. Belyaeva & M. Elgeti 10.7554/eLife.99770
- Time-resolved DEER EPR and solid-state NMR afford kinetic and structural elucidation of substrate binding to Ca 2+ -ligated calmodulin T. Schmidt et al. 10.1073/pnas.2122308119
- Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding C. Wiedemann et al. 10.1016/j.ijbiomac.2023.126366
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- DEER Analysis of GPCR Conformational Heterogeneity M. Elgeti & W. Hubbell 10.3390/biom11060778
- Accessing the triplet state of perylenediimide by radical-enhanced intersystem crossing M. Mayländer et al. 10.1039/D2SC01899C
- Simultaneous Localization of Two High Affinity Divalent Metal Ion Binding Sites in the Tetracycline RNA Aptamer with Mn2+-Based Pulsed Dipolar EPR Spectroscopy T. Hetzke et al. 10.1021/acs.jpclett.3c02566
- Increasing the Modulation Depth of GdIII-Based Pulsed Dipolar EPR Spectroscopy (PDS) with Porphyrin–GdIII Laser-Induced Magnetic Dipole Spectroscopy A. Scherer et al. 10.1021/acs.jpclett.2c02138
- Activation of Csm6 ribonuclease by cyclic nucleotide binding: in an emergency, twist to open S. McQuarrie et al. 10.1093/nar/gkad739
- Direct Comparison between Förster Resonance Energy Transfer and Light-Induced Triplet–Triplet Electron Resonance Spectroscopy A. Bertran et al. 10.1021/jacs.3c04685
- A new 13C trityl-based spin label enables the use of DEER for distance measurements Z. Hasanbasri et al. 10.1016/j.jmr.2022.107363
- MMM: Integrative ensemble modeling and ensemble analysis G. Jeschke 10.1002/pro.3965
- Electron paramagnetic resonance spectroscopy on G-protein-coupled receptors: Adopting strategies from related model systems J. Reichenwallner et al. 10.1016/j.sbi.2021.06.003
- Antiviral signalling by a cyclic nucleotide activated CRISPR protease C. Rouillon et al. 10.1038/s41586-022-05571-7
- Monitoring the conformational ensemble and lipid environment of a mechanosensitive channel under cyclodextrin-induced membrane tension B. Lane et al. 10.1016/j.str.2024.02.020
- Differentiating between Label and Protein Conformers in Pulsed Dipolar EPR Spectroscopy with the dHis‐Cu2+(NTA) Motif C. Heubach et al. 10.1002/chem.202302541
- CRISPR antiphage defence mediated by the cyclic nucleotide-binding membrane protein Csx23 S. Grüschow et al. 10.1093/nar/gkae167
- Regularized dynamical decoupling noise spectroscopy – a decoherence descriptor for radicals in glassy matrices J. Soetbeer et al. 10.1039/D1CP03103A
- End-to-End Distance Probability Distributions of Dilute Poly(ethylene oxide) in Aqueous Solution N. Sherck et al. 10.1021/jacs.0c08709
- The use of EPR spectroscopy to study transcription mechanisms L. Hofmann et al. 10.1007/s12551-022-01004-x
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- Bayesian Probabilistic Inference of Nonparametric Distance Distributions in DEER Spectroscopy S. Sweger et al. 10.1021/acs.jpca.4c05056
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- The effect of spin-lattice relaxation on DEER background decay M. Seal et al. 10.1016/j.jmr.2022.107327
- Probing Structural Dynamics of Membrane Proteins Using Electron Paramagnetic Resonance Spectroscopic Techniques I. Sahu & G. Lorigan 10.3390/biophysica1020009
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- Direct observation of negative cooperativity in a detoxification enzyme at the atomic level by Electron Paramagnetic Resonance spectroscopy and simulation X. Bogetti et al. 10.1002/pro.4770
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- Time‐Resolved Mn2+−NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter** M. Rudolph et al. 10.1002/anie.202307091
- Dynamical decoupling in water–glycerol glasses: a comparison of nitroxides, trityl radicals and gadolinium complexes J. Soetbeer et al. 10.1039/D1CP00055A
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87 citations as recorded by crossref.
- Trendbericht: Elektronen‐Paramagnetische‐Resonanzspektroskopie O. Schiemann 10.1002/nadc.20214106853
- In-cell investigation of the conformational landscape of the GTPase UreG by SDSL-EPR A. Pierro et al. 10.1016/j.isci.2023.107855
- Modeling of Cu(ii)-based protein spin labels using rotamer libraries Z. Hasanbasri et al. 10.1039/D3CP05951K
- Deconvoluting Monomer- and Dimer-Specific Distance Distributions between Spin Labels in a Monomer/Dimer Mixture Using T1-Edited DEER EPR Spectroscopy T. Schmidt et al. 10.1021/jacs.4c03916
- PDSFit: PDS data analysis in the presence of orientation selectivity, g‐anisotropy, and exchange coupling D. Abdullin et al. 10.1002/mrc.5415
- Spin Labeling of RNA Using “Click” Chemistry for Coarse-grained Structure Determination via Pulsed Electron-electron Double Resonance Spectroscopy M. Vicino et al. 10.21769/BioProtoc.4004
- Lateral gating mechanism and plasticity of the β-barrel assembly machinery complex in micelles and Escherichia coli A. Gopinath et al. 10.1093/pnasnexus/pgae019
- Quantifying Polypeptoid Conformational Landscapes through Integrated Experiment and Simulation S. Jiao et al. 10.1021/acs.macromol.1c00550
- Estimation of Distance Distributions Between Gd3+ Ion Pairs with a Significant Zero-Field Splitting from Pulsed EPR DEER Data S. Misra & H. Salahi 10.1007/s00723-022-01521-8
- Confidence limits in pulse dipolar EPR spectroscopy: estimates for individual measurements V. Syryamina et al. 10.1039/D3CP05797F
- An optimal acquisition scheme for Q-band EPR distance measurements using Cu2+-based protein labels X. Bogetti et al. 10.1039/D2CP01032A
- Design of stimulus-responsive two-state hinge proteins F. Praetorius et al. 10.1126/science.adg7731
- Quantifying methyl tunneling induced (de)coherence of nitroxides in glassy ortho-terphenyl at low temperatures A. Eggeling et al. 10.1039/D3CP01299A
- Ensemble structure of the N-terminal domain (1–267) of FUS in a biomolecular condensate L. Esteban-Hofer et al. 10.1016/j.bpj.2024.01.023
- Methodology for rigorous modeling of protein conformational changes by Rosetta using DEER distance restraints D. del Alamo et al. 10.1371/journal.pcbi.1009107
- Cross-validation of distance measurements in proteins by PELDOR/DEER and single-molecule FRET M. Peter et al. 10.1038/s41467-022-31945-6
- Membrane potential accelerates sugar uptake by stabilizing the outward facing conformation of the Na/glucose symporter vSGLT F. Khan et al. 10.1038/s41467-023-43119-z
- Entschlüsselung der ligandeninduzierten Verdrehung eines homodimeren Enzyms mit Hilfe der gepulsten Elektron‐Elektron‐Doppelresonanz‐Spektroskopie D. Nguyen et al. 10.1002/ange.202108179
- Insights into the Conformational Plasticity of the Protein Kinase Akt1 by Multi‐Lateral Dipolar Spectroscopy J. Stehle et al. 10.1002/chem.202203959
- Enhanced sensitivity for pulse dipolar EPR spectroscopy using variable-time RIDME J. Wort et al. 10.1016/j.jmr.2023.107460
- Pulsed EPR Methods in the Angstrom to Nanometre Scale Shed Light on the Conformational Flexibility of a Fluoride Riboswitch L. Remmel et al. 10.1002/anie.202411241
- Electron paramagnetic resonance spectroscopy in structural-dynamic studies of large protein complexes L. Galazzo & E. Bordignon 10.1016/j.pnmrs.2022.11.001
- Dipolar pathways in dipolar EPR spectroscopy L. Fábregas-Ibáñez et al. 10.1039/D1CP03305K
- Protein delivery to living cells by thermal stimulation for biophysical investigation F. Torricella et al. 10.1038/s41598-022-21103-9
- In situ distance measurements in a membrane transporter using maleimide functionalized orthogonal spin labels and 5-pulse electron-electron double resonance spectroscopy S. Ketter et al. 10.1016/j.jmro.2022.100041
- Measuring conformational equilibria in allosteric proteins with time-resolved tmFRET W. Zagotta et al. 10.1016/j.bpj.2024.01.033
- Dynamic basis of lipopolysaccharide export by LptB2FGC M. Dajka et al. 10.7554/eLife.99338.3
- Zeitaufgelöste Mn2+−NO‐ und NO−NO‐Abstandsmessungen zeigen regulierende Funktion der katalytischen Asymmetrie auf den alternierenden Zugang in einem ABC‐Transporter** M. Rudolph et al. 10.1002/ange.202307091
- Unraveling a Ligand‐Induced Twist of a Homodimeric Enzyme by Pulsed Electron–Electron Double Resonance D. Nguyen et al. 10.1002/anie.202108179
- Exploring tunneling ESEEM beyond methyl groups in nitroxides at low temperatures A. Eggeling et al. 10.1039/D4CP01212G
- Puls EPR Methoden im Angstöm‐ bis Nanometerbereich geben Aufschluss über die konformationelle Flexibilität eines Fluorid‐Riboschalters L. Remmel et al. 10.1002/ange.202411241
- Protein functional dynamics from the rigorous global analysis of DEER data: Conditions, components, and conformations E. Hustedt et al. 10.1085/jgp.201711954
- Dipolar pathways in multi-spin and multi-dimensional dipolar EPR spectroscopy L. Fábregas-Ibáñez et al. 10.1039/D2CP03048A
- EPR spectroscopic characterisation of native CuII-binding sites in human serum albumin K. Ackermann et al. 10.1039/D4DT00892H
- Enzymatic Spin-Labeling of Protein N- and C-Termini for Electron Paramagnetic Resonance Spectroscopy R. Dunleavy et al. 10.1021/acs.bioconjchem.3c00029
- Exploring protein structural ensembles: Integration of sparse experimental data from electron paramagnetic resonance spectroscopy with molecular modeling methods J. Belyaeva & M. Elgeti 10.7554/eLife.99770
- Time-resolved DEER EPR and solid-state NMR afford kinetic and structural elucidation of substrate binding to Ca 2+ -ligated calmodulin T. Schmidt et al. 10.1073/pnas.2122308119
- Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding C. Wiedemann et al. 10.1016/j.ijbiomac.2023.126366
- EPR Spectroscopy Provides New Insights into Complex Biological Reaction Mechanisms L. Hofmann & S. Ruthstein 10.1021/acs.jpcb.2c05235
- Gd3+–Trityl–Nitroxide Triple Labeling and Distance Measurements in the Heterooligomeric Cobalamin Transport Complex in the Native Lipid Bilayers S. Ketter & B. Joseph 10.1021/jacs.2c10080
- A DNA unwinding equilibrium serves as a checkpoint for CRISPR-Cas12a target discrimination J. Singh et al. 10.1093/nar/gkad636
- Compactness regularization in the analysis of dipolar EPR spectroscopy data L. Fábregas-Ibáñez et al. 10.1016/j.jmr.2022.107218
- Ligand-specific conformational change drives interdomain allostery in Pin1 A. Born et al. 10.1038/s41467-022-32340-x
- Benchmark Test and Guidelines for DEER/PELDOR Experiments on Nitroxide-Labeled Biomolecules O. Schiemann et al. 10.1021/jacs.1c07371
- DEER Analysis of GPCR Conformational Heterogeneity M. Elgeti & W. Hubbell 10.3390/biom11060778
- Accessing the triplet state of perylenediimide by radical-enhanced intersystem crossing M. Mayländer et al. 10.1039/D2SC01899C
- Simultaneous Localization of Two High Affinity Divalent Metal Ion Binding Sites in the Tetracycline RNA Aptamer with Mn2+-Based Pulsed Dipolar EPR Spectroscopy T. Hetzke et al. 10.1021/acs.jpclett.3c02566
- Increasing the Modulation Depth of GdIII-Based Pulsed Dipolar EPR Spectroscopy (PDS) with Porphyrin–GdIII Laser-Induced Magnetic Dipole Spectroscopy A. Scherer et al. 10.1021/acs.jpclett.2c02138
- Activation of Csm6 ribonuclease by cyclic nucleotide binding: in an emergency, twist to open S. McQuarrie et al. 10.1093/nar/gkad739
- Direct Comparison between Förster Resonance Energy Transfer and Light-Induced Triplet–Triplet Electron Resonance Spectroscopy A. Bertran et al. 10.1021/jacs.3c04685
- A new 13C trityl-based spin label enables the use of DEER for distance measurements Z. Hasanbasri et al. 10.1016/j.jmr.2022.107363
- MMM: Integrative ensemble modeling and ensemble analysis G. Jeschke 10.1002/pro.3965
- Electron paramagnetic resonance spectroscopy on G-protein-coupled receptors: Adopting strategies from related model systems J. Reichenwallner et al. 10.1016/j.sbi.2021.06.003
- Antiviral signalling by a cyclic nucleotide activated CRISPR protease C. Rouillon et al. 10.1038/s41586-022-05571-7
- Monitoring the conformational ensemble and lipid environment of a mechanosensitive channel under cyclodextrin-induced membrane tension B. Lane et al. 10.1016/j.str.2024.02.020
- Differentiating between Label and Protein Conformers in Pulsed Dipolar EPR Spectroscopy with the dHis‐Cu2+(NTA) Motif C. Heubach et al. 10.1002/chem.202302541
- CRISPR antiphage defence mediated by the cyclic nucleotide-binding membrane protein Csx23 S. Grüschow et al. 10.1093/nar/gkae167
- Regularized dynamical decoupling noise spectroscopy – a decoherence descriptor for radicals in glassy matrices J. Soetbeer et al. 10.1039/D1CP03103A
- End-to-End Distance Probability Distributions of Dilute Poly(ethylene oxide) in Aqueous Solution N. Sherck et al. 10.1021/jacs.0c08709
- The use of EPR spectroscopy to study transcription mechanisms L. Hofmann et al. 10.1007/s12551-022-01004-x
- Solution-State Inter-Copper Distribution of Redox Partner-Linked Copper Nitrite Reductases: A Pulsed Electron–Electron Double Resonance Spectroscopy Study T. Hedison et al. 10.1021/acs.jpclett.2c01584
- Bayesian Probabilistic Inference of Nonparametric Distance Distributions in DEER Spectroscopy S. Sweger et al. 10.1021/acs.jpca.4c05056
- Comparative evaluation of spin-label modeling methods for protein structural studies M. Tessmer et al. 10.1016/j.bpj.2022.08.002
- The effect of spin-lattice relaxation on DEER background decay M. Seal et al. 10.1016/j.jmr.2022.107327
- Probing Structural Dynamics of Membrane Proteins Using Electron Paramagnetic Resonance Spectroscopic Techniques I. Sahu & G. Lorigan 10.3390/biophysica1020009
- DEER Data Analysis Software: A Comparative Guide H. Russell et al. 10.3389/fmolb.2022.915167
- Direct observation of negative cooperativity in a detoxification enzyme at the atomic level by Electron Paramagnetic Resonance spectroscopy and simulation X. Bogetti et al. 10.1002/pro.4770
- NMR and EPR reveal a compaction of the RNA-binding protein FUS upon droplet formation L. Emmanouilidis et al. 10.1038/s41589-021-00752-3
- Characterization of Weak Protein Domain Structure by Spin-Label Distance Distributions I. Ritsch et al. 10.3389/fmolb.2021.636599
- Quantitative analysis of sterol-modulated monomer–dimer equilibrium of the β 1 -adrenergic receptor by DEER spectroscopy N. Kubatova et al. 10.1073/pnas.2221036120
- The effect of the zero-field splitting in light-induced pulsed dipolar electron paramagnetic resonance (EPR) spectroscopy A. Scherer et al. 10.5194/mr-4-27-2023
- Impact of Cellular Crowding on Protein Structural Dynamics Investigated by EPR Spectroscopy A. Pierro et al. 10.1021/acs.chemrev.3c00951
- Quantitative Agreement between Conformational Substates of Holo Calcium-Loaded Calmodulin Detected by Double Electron–Electron Resonance EPR and Predicted by Molecular Dynamics Simulations T. Schmidt et al. 10.1021/jacs.2c02201
- Efficient sampling of molecular orientations for Cu(ii)-based DEER on protein labels Z. Hasanbasri et al. 10.1039/D3CP00404J
- A Comparison of Cysteine-Conjugated Nitroxide Spin Labels for Pulse Dipolar EPR Spectroscopy K. Ackermann et al. 10.3390/molecules26247534
- Site-Specific Labeling Reveals Cas9 Induces Partial Unwinding Without RNA/DNA Pairing in Sequences Distal to the PAM Y. Li et al. 10.1089/crispr.2021.0100
- A Rotamer Library Approach to Modeling Side Chain Ensembles of the Bifunctional Spin Label RX M. Tessmer & S. Stoll 10.1007/s00723-023-01576-1
- Differentiating Unimodal and Multimodal Distributions in Pulsed Dipolar Spectroscopy Using Wavelet Transforms A. Sinha Roy et al. 10.1007/s00723-023-01616-w
- Determining electron–nucleus distances and Fermi contact couplings from ENDOR spectra S. Pribitzer et al. 10.1039/D1CP00229E
- Temperature-Dependent Rotation of Protonated Methyl Groups in Otherwise Deuterated Proteins Modulates DEER Distance Distributions T. Schmidt & V. Stadnytskyi 10.1007/s00723-024-01720-5
- Ligand efficacy modulates conformational dynamics of the µ-opioid receptor J. Zhao et al. 10.1038/s41586-024-07295-2
- Time‐Resolved Mn2+−NO and NO−NO Distance Measurements Reveal That Catalytic Asymmetry Regulates Alternating Access in an ABC Transporter** M. Rudolph et al. 10.1002/anie.202307091
- Dynamical decoupling in water–glycerol glasses: a comparison of nitroxides, trityl radicals and gadolinium complexes J. Soetbeer et al. 10.1039/D1CP00055A
- Neural networks in pulsed dipolar spectroscopy: A practical guide J. Keeley et al. 10.1016/j.jmr.2022.107186
- Titin UN2A Acts as a Stable, Non‐Polymorphic Scaffold in its Binding to CARP J. Stehle et al. 10.1002/cbic.202300408
- Conducting a three-pulse DEER experiment without dead time: A review S. Dzuba 10.1016/j.jmro.2023.100100
- Structural insights into the semiquinone form of human Cytochrome P450 reductase by DEER distance measurements between a native flavin and a spin labelled non‐canonical amino acid M. Bizet et al. 10.1002/chem.202304307
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Latest update: 23 Nov 2024
Short summary
Dipolar electron paramagnetic resonance spectroscopy methods such as DEER provide data on how proteins change shape, thus giving detailed insight into how proteins work. We present DeerLab, a comprehensive open-source software for reliably analyzing the associated data. The software implements a series of theoretical and algorithmic innovations and thereby improves the quality and reproducibility of data analysis.
Dipolar electron paramagnetic resonance spectroscopy methods such as DEER provide data on how...