Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 18, Issue 8, Pages 5799-5806Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5cp04753f
Keywords
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Funding
- EPSRC, iMR-CDT
- MRC UK [G1100021]
- EPSRC Basic Technology [EP/F039034/1]
- Wellcome Trust [099149/Z/12/Z]
- Engineering and Physical Sciences Research Council [EP/F039034/1, 1115730] Funding Source: researchfish
- Medical Research Council [G1100021] Funding Source: researchfish
- Wellcome Trust [095062/Z/10/Z] Funding Source: researchfish
- EPSRC [EP/F039034/1] Funding Source: UKRI
- MRC [G1100021] Funding Source: UKRI
- Wellcome Trust [095062/Z/10/Z] Funding Source: Wellcome Trust
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The bipedal spin label Rx is more restricted in its conformation and dynamics than its monopodal counterpart R1. To systematically investigate the utility of the Rx label, we have attempted to comprehensively survey the attachment of Rx to protein secondary structures. We have examined the formation, structure and dynamics of the spin label in relation to the underlying protein in order to determine feasibility and optimum conditions for distance and orientation measurement by pulsed EPR. The labeled proteins have been studied using molecular dynamics, CW EPR, pulsed EPR distance measurement at X-band and orientation measurement at W-band. The utility of different modes and positions of attachment have been compared and contrasted.
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