Differentiation of direct and remote connectivities in phase-sensitive double-quantum spectra of proteins by variation of the multiple-quantum excitation period

1986 ◽  
Vol 69 (2) ◽  
pp. 356-361 ◽  
Author(s):  
Claudio Dalvit ◽  
Mark Rance ◽  
Peter E Wright
2019 ◽  
Author(s):  
Michelle Gill ◽  
Andrew Hsu ◽  
Arthur G. Palmer, III

<div> <div> <div> <p>The zero- and double-quantum methyl TROSY Hahn-echo and the methyl <sup>1</sup>H-<sup>1</sup>H dipole- dipole cross-correlation nuclear magnetic resonance experiments enable estimation of multiple quantum chemical exchange broadening in methyl groups in proteins. The two relaxation rate constants are established to be linearly dependent using molecular dynamics simulations and empirical analysis of experimental data. This relationship allows chemical exchange broadening to be recognized as an increase in the Hahn-echo relaxation rate constant. The approach is illustrated by analyzing relaxation data collected at three temperatures for <i>E. coli </i>ribonuclease HI and by analyzing relaxation data collected for different cofactor and substrate complexes of <i>E. coli </i>AlkB. </p> </div> </div> </div>


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