ISSN:
1573-5001
Keywords:
calmodulin
;
HCANH
;
multiple quantum line narrowing
;
NMR assignment
;
resolution
;
SEF2-1
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract We report a 3D constant-time HCANH experiment (CTSL-HCANH) that uses the slower relaxation of multiple-quantum coherence to increase sensitivity and provides high Cα resolution. In this experiment the Hα of the (Hα, Cα) multiple quanta are selectively spin locked, so that Hα chemical shift evolution and 1 H-1H J-dephasing become ineffective during the relatively long delay needed for Cα to N coherence transfer. As compared to an HCANH experiment that uses Cα single-quantum coherence, an average enhancement of 20% was observed on calmodulin in complex with the binding domain of the transcription factor SEF2-1. Compared to CBCANH the signal intensity is approximately twice as good. The favorable relaxation properties of multiple quanta, together with the outstanding Cα resolution, make the experiment a very good complement to CBCANH and CBCA(CO)NH for sequential assignment of larger proteins for which deuteration is not yet necessary.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008308307363
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