Dependence of distance distributions derived from double electron-electron resonance pulsed EPR spectroscopy on pulse-sequence time

Angewandte Chemie
James L BaberG Marius Clore

Abstract

Pulsed double electron-electron resonance (DEER) provides pairwise P(r) distance distributions in doubly spin labeled proteins. We report that in protonated proteins, P(r) is dependent on the length of the second echo period T owing to local environmental effects on the spin-label phase memory relaxation time Tm . For the protein ABD, this effect results in a 1.4 Å increase in the P(r) maximum from T=6 to 20 μs. Protein A has a bimodal P(r) distribution, and the relative height of the shorter distance peak at T=10 μs, the shortest value required to obtain a reliable P(r), is reduced by 40 % relative to that found by extrapolation to T=0. Our results indicate that data at a series of T values are essential for quantitative interpretation of DEER to determine the extent of the T dependence and to extrapolate the results to T=0. Complete deuteration (99 %) of the protein was accompanied by a significant increase in Tm and effectively abolished the P(r) dependence on T.

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Citations

Dec 30, 2016·The Journal of Organic Chemistry·Shengdian HuangAndrzej Rajca
Jul 22, 2016·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Thomas SchmidtG Marius Clore
Oct 7, 2016·Physical Chemistry Chemical Physics : PCCP·Katharina KellerMaxim Yulikov
Mar 29, 2019·Physical Chemistry Chemical Physics : PCCP·Katharina KellerMaxim Yulikov
Sep 18, 2020·Chemical Communications : Chem Comm·Thomas Schmidt, G Marius Clore
Aug 7, 2019·Proceedings of the National Academy of Sciences of the United States of America·Thomas SchmidtG Marius Clore
Apr 5, 2017·Proceedings of the National Academy of Sciences of the United States of America·Ned Van EpsWayne L Hubbell
May 10, 2020·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Thomas SchmidtG Marius Clore

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