title: EPR distance measurements in deuterated proteins.
abstract: One of the major problems facing distance determination by pulsed EPR, on spin-labeled proteins, has been the short relaxation time T(m). Solvent deuteration has previously been used to slow relaxation and so extend the range of distance measurement and sensitivity. We demonstrate here that deuteration of the underlying protein, as well as the solvent, extends the T(m) to a considerable degree. Longer T(m) gives greatly enhanced sensitivity, much extended distance measurement, more reliable distance distribution calculation and better baseline correction.
authors.affiliation: School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
authors.forename: Richard
authors.initials: R
authors.lastname: Ward
authors.forename: Andrew
authors.initials: A
authors.lastname: Bowman
authors.forename: Erman
authors.initials: E
authors.lastname: Sozudogru
authors.forename: Hassane
authors.initials: H
authors.lastname: El-Mkami
authors.forename: Tom
authors.initials: T
authors.lastname: Owen-Hughes
authors.forename: David G
authors.initials: DG
authors.lastname: Norman
mesh_terms: D000465:Algorithms; D001419:Bacteria / Q000254:growth & development; D003903:Deuterium / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D006657:Histones / Q000737:chemistry / Q000302:isolation & purification; D007553:Isotope Labeling; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification; D012997:Solvents; D013113:Spin Labels
chemical_list: D006657:Histones; D011506:Proteins; D012997:Solvents; D013113:Spin Labels; D003903:Deuterium
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