Estimates of methyl 13C and 1H CSA values (Deltasigma) in proteins from cross-correlated spin relaxation.

Abstract:

:Simple pulse schemes are presented for the measurement of methyl (13)C and (1)H CSA values from (1)H-(13)C dipole/(13)C CSA and (1)H-(13)C dipole/(1)H CSA cross-correlated relaxation. The methodology is applied to protein L and malate synthase G. Average (13)C CSA values are considerably smaller for Ile than Leu/Val (17 vs 25 ppm) and are in good agreement with previous solid state NMR studies of powders of amino acids and dipeptides and in reasonable agreement with quantum-chemical DFT calculations of methyl carbon CSA values in peptide fragments. Small averaged (1)H CSA values on the order of 1 ppm are measured, consistent with a solid state NMR determination of the methyl group (1)H CSA in dimethylmalonic acid.

journal_name

J Biomol NMR

authors

Tugarinov V,Scheurer C,Brüschweiler R,Kay LE

doi

10.1007/s10858-004-4349-x

subject

Has Abstract

pub_date

2004-12-01 00:00:00

pages

397-406

issue

4

eissn

0925-2738

issn

1573-5001

journal_volume

30

pub_type

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