13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics.

A pulse scheme is presented for quantifying millisecond time scale chemical exchange processes in proteins by measuring (1)H CPMG relaxation dispersion profiles of (13)CHD(2) methyl groups. The use of (13)CHD(2) isotopomers for (1)H methyl dispersion experiments eliminates problems with interconvers...

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Main Authors: Baldwin, A, Religa, T, Hansen, D, Bouvignies, G, Kay, L
Format: Journal article
Language:English
Published: 2010
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author Baldwin, A
Religa, T
Hansen, D
Bouvignies, G
Kay, L
author_facet Baldwin, A
Religa, T
Hansen, D
Bouvignies, G
Kay, L
author_sort Baldwin, A
collection OXFORD
description A pulse scheme is presented for quantifying millisecond time scale chemical exchange processes in proteins by measuring (1)H CPMG relaxation dispersion profiles of (13)CHD(2) methyl groups. The use of (13)CHD(2) isotopomers for (1)H methyl dispersion experiments eliminates problems with interconversion between differentially relaxing proton transitions that complicate the extraction of accurate exchange parameters when (13)CH(3) probes are used. Good agreement is demonstrated between extracted chemical shift differences from fits of dispersion profiles and the corresponding differences measured independently on a model exchanging system, validating the experiment. The methodology is applied to the gating residues of the T. acidiphilium proteasome that are shown to undergo extensive motion on the millisecond time scale.
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spelling oxford-uuid:d9278129-bc31-452f-b0ba-71c89a43c79b2022-03-27T08:53:51Z13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d9278129-bc31-452f-b0ba-71c89a43c79bEnglishSymplectic Elements at Oxford2010Baldwin, AReliga, THansen, DBouvignies, GKay, LA pulse scheme is presented for quantifying millisecond time scale chemical exchange processes in proteins by measuring (1)H CPMG relaxation dispersion profiles of (13)CHD(2) methyl groups. The use of (13)CHD(2) isotopomers for (1)H methyl dispersion experiments eliminates problems with interconversion between differentially relaxing proton transitions that complicate the extraction of accurate exchange parameters when (13)CH(3) probes are used. Good agreement is demonstrated between extracted chemical shift differences from fits of dispersion profiles and the corresponding differences measured independently on a model exchanging system, validating the experiment. The methodology is applied to the gating residues of the T. acidiphilium proteasome that are shown to undergo extensive motion on the millisecond time scale.
spellingShingle Baldwin, A
Religa, T
Hansen, D
Bouvignies, G
Kay, L
13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics.
title 13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics.
title_full 13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics.
title_fullStr 13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics.
title_full_unstemmed 13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics.
title_short 13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics.
title_sort 13chd2 methyl group probes of millisecond time scale exchange in proteins by 1h relaxation dispersion an application to proteasome gating residue dynamics
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AT hansend 13chd2methylgroupprobesofmillisecondtimescaleexchangeinproteinsby1hrelaxationdispersionanapplicationtoproteasomegatingresiduedynamics
AT bouvigniesg 13chd2methylgroupprobesofmillisecondtimescaleexchangeinproteinsby1hrelaxationdispersionanapplicationtoproteasomegatingresiduedynamics
AT kayl 13chd2methylgroupprobesofmillisecondtimescaleexchangeinproteinsby1hrelaxationdispersionanapplicationtoproteasomegatingresiduedynamics