ISSN:
1573-5001
Schlagwort(e):
adiabatic decoupling
;
bicelles
;
homonuclear decoupling
;
protein alignment
;
residual dipolar coupling
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
,
Chemie und Pharmazie
Notizen:
Abstract Residual heteronuclear dipolar couplings obtained from partially oriented protein samples can provide unique NMR constraints for protein structure determination. However, partial orientation of protein samples also causes severe 1 H line broadening resulting from residual 1 H-1H dipolar couplings. In this communication we show that band-selective 1H homonuclear decoupling during data acquisition is an efficient way to suppress residual 1H-1H dipolar couplings, resulting in spectra that are still amenable to solution NMR analysis, even with high degrees of alignment. As an example, we present a novel experiment with improved sensitivity for the measurement of one-bond 1 HN-15N residual dipolar couplings in a protein sample dissolved in magnetically aligned liquid crystalline bicelles.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1023/A:1008387305293
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