Toolkit/high-field/high-frequency EPR
high-field/high-frequency EPR
Also known as: high-field EPR, high-frequency EPR
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
By combining site-directed spin labeling with high-field/high-frequency EPR, unique information on the proteins is revealed... Taking advantage of the improved spectral and temporal resolution of high-field EPR at 95 GHz/3.4 T and 360 GHz/12.9 T, as compared to conventional X-band EPR (9.5 GHz/0.34 T), detailed information on the transient intermediates of the proteins in biological action is obtained.
Usefulness & Problems
Why this is useful
High-field/high-frequency EPR provides improved spectral and temporal resolution for studying proteins in action, including transient intermediates. In this paper it is explicitly paired with site-directed spin labeling.; obtaining detailed information on transient protein intermediates; probing site-specific microenvironment features such as hydrogen-bonding and polarity effects; characterizing proteins in working states on biologically relevant timescales
Source:
High-field/high-frequency EPR provides improved spectral and temporal resolution for studying proteins in action, including transient intermediates. In this paper it is explicitly paired with site-directed spin labeling.
Source:
obtaining detailed information on transient protein intermediates
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probing site-specific microenvironment features such as hydrogen-bonding and polarity effects
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characterizing proteins in working states on biologically relevant timescales
Problem solved
It addresses the need for more detailed characterization of transient intermediates and site-specific microenvironment changes than conventional X-band EPR provides.; improves spectral and temporal resolution relative to conventional X-band EPR
Source:
It addresses the need for more detailed characterization of transient intermediates and site-specific microenvironment changes than conventional X-band EPR provides.
Source:
improves spectral and temporal resolution relative to conventional X-band EPR
Problem links
improves spectral and temporal resolution relative to conventional X-band EPR
LiteratureIt addresses the need for more detailed characterization of transient intermediates and site-specific microenvironment changes than conventional X-band EPR provides.
Source:
It addresses the need for more detailed characterization of transient intermediates and site-specific microenvironment changes than conventional X-band EPR provides.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
electron paramagnetic resonance detectionnitroxide spin labelingsite-directed spin labelingTarget processes
No target processes tagged yet.
Implementation Constraints
The abstract explicitly mentions operation at 95 GHz/3.4 T and 360 GHz/12.9 T, indicating specialized high-field EPR instrumentation is required.; requires high-field/high-frequency EPR instrumentation; often used in combination with site-directed spin labeling
Uses more than one coordinated component. Independent follow-up evidence is still limited. Validation breadth across biological contexts is still narrow. Independent reuse still looks limited, so the evidence base may be fragile. Multi-component delivery and stoichiometry control can make deployment harder. No canonical validation observations are stored yet, so context-specific performance remains under-specified.
Validation
Supporting Sources
Ranked Claims
High-field EPR experiments with pH-sensitive nitroxide spin labels can be used to probe site-specific pK(a) values in protein systems.
to report on novel high-field EPR experiments for probing site-specific pK(a) values in protein systems by means of pH-sensitive nitroxide spin labels
Combining site-directed spin labeling with high-field/high-frequency EPR reveals unique information on proteins that is complementary to X-ray crystallography, solid-state NMR, FRET, and fast infrared and optical spectroscopic techniques.
By combining site-directed spin labeling with high-field/high-frequency EPR, unique information on the proteins is revealed, which is complementary to that of X-ray crystallography, solid-state NMR, FRET, fast infrared and optical spectroscopic techniques.
High-field EPR can obtain detailed information on transient intermediates of proteins in biological action and can observe and characterize these intermediates while they remain in working states on biologically relevant timescales.
detailed information on the transient intermediates of the proteins in biological action is obtained. These intermediates can be observed and characterized while staying in their working states on biologically relevant timescales.
Site-directed spin labeling with suitable nitroxide radicals allows EPR to study protein structure and conformational dynamics even when the transfer process lacks stable or transient paramagnetic species or states.
In case the transfer process does not involve stable or transient paramagnetic species or states, site-directed spin labeling with suitable nitroxide radicals still allows EPR techniques to be used for studying structure and conformational dynamics of the proteins in action.
High-field EPR at 95 GHz/3.4 T and 360 GHz/12.9 T provides improved spectral and temporal resolution compared with conventional X-band EPR at 9.5 GHz/0.34 T.
Taking advantage of the improved spectral and temporal resolution of high-field EPR at 95 GHz/3.4 T and 360 GHz/12.9 T, as compared to conventional X-band EPR (9.5 GHz/0.34 T)
Approval Evidence
By combining site-directed spin labeling with high-field/high-frequency EPR, unique information on the proteins is revealed... Taking advantage of the improved spectral and temporal resolution of high-field EPR at 95 GHz/3.4 T and 360 GHz/12.9 T, as compared to conventional X-band EPR (9.5 GHz/0.34 T), detailed information on the transient intermediates of the proteins in biological action is obtained.
Source:
High-field EPR experiments with pH-sensitive nitroxide spin labels can be used to probe site-specific pK(a) values in protein systems.
to report on novel high-field EPR experiments for probing site-specific pK(a) values in protein systems by means of pH-sensitive nitroxide spin labels
Source:
Combining site-directed spin labeling with high-field/high-frequency EPR reveals unique information on proteins that is complementary to X-ray crystallography, solid-state NMR, FRET, and fast infrared and optical spectroscopic techniques.
By combining site-directed spin labeling with high-field/high-frequency EPR, unique information on the proteins is revealed, which is complementary to that of X-ray crystallography, solid-state NMR, FRET, fast infrared and optical spectroscopic techniques.
Source:
High-field EPR can obtain detailed information on transient intermediates of proteins in biological action and can observe and characterize these intermediates while they remain in working states on biologically relevant timescales.
detailed information on the transient intermediates of the proteins in biological action is obtained. These intermediates can be observed and characterized while staying in their working states on biologically relevant timescales.
Source:
High-field EPR at 95 GHz/3.4 T and 360 GHz/12.9 T provides improved spectral and temporal resolution compared with conventional X-band EPR at 9.5 GHz/0.34 T.
Taking advantage of the improved spectral and temporal resolution of high-field EPR at 95 GHz/3.4 T and 360 GHz/12.9 T, as compared to conventional X-band EPR (9.5 GHz/0.34 T)
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Comparisons
Source-stated alternatives
The abstract contrasts it with conventional X-band EPR and says its information is complementary to X-ray crystallography, solid-state NMR, FRET, and fast infrared and optical spectroscopic techniques.
Source:
The abstract contrasts it with conventional X-band EPR and says its information is complementary to X-ray crystallography, solid-state NMR, FRET, and fast infrared and optical spectroscopic techniques.
Source-backed strengths
reveals unique information complementary to other structural and spectroscopic methods; improved spectral and temporal resolution at 95 GHz/3.4 T and 360 GHz/12.9 T
Source:
reveals unique information complementary to other structural and spectroscopic methods
Source:
improved spectral and temporal resolution at 95 GHz/3.4 T and 360 GHz/12.9 T
Compared with FRET
The abstract contrasts it with conventional X-band EPR and says its information is complementary to X-ray crystallography, solid-state NMR, FRET, and fast infrared and optical spectroscopic techniques.
Shared frame: source-stated alternative in extracted literature
Strengths here: reveals unique information complementary to other structural and spectroscopic methods; improved spectral and temporal resolution at 95 GHz/3.4 T and 360 GHz/12.9 T.
Source:
The abstract contrasts it with conventional X-band EPR and says its information is complementary to X-ray crystallography, solid-state NMR, FRET, and fast infrared and optical spectroscopic techniques.
Compared with X-ray crystallography
The abstract contrasts it with conventional X-band EPR and says its information is complementary to X-ray crystallography, solid-state NMR, FRET, and fast infrared and optical spectroscopic techniques.
Shared frame: source-stated alternative in extracted literature
Strengths here: reveals unique information complementary to other structural and spectroscopic methods; improved spectral and temporal resolution at 95 GHz/3.4 T and 360 GHz/12.9 T.
Source:
The abstract contrasts it with conventional X-band EPR and says its information is complementary to X-ray crystallography, solid-state NMR, FRET, and fast infrared and optical spectroscopic techniques.
Ranked Citations
- 1.