Sensitivity enhanced NMR spectroscopy by quenching scalar coupling mediated relaxation: Application to the direct observation of hydrogen bonds in 13C/15N-labeled proteins Journal Article

  

Authors:	Liu, A.; Hu, W.; Qamar, S.; Majumdar, A.
Article Title:	Sensitivity enhanced NMR spectroscopy by quenching scalar coupling mediated relaxation: Application to the direct observation of hydrogen bonds in 13C/15N-labeled proteins
Abstract:	In this paper, we demonstrate that the sensitivity of triple-resonance NMR experiments can be enhanced significantly through quenching scalar coupling mediated relaxation by using composite-pulse decoupling (CPD) or an adiabatic decoupling sequence on aliphatic, in particular alpha-carbons in 13C/15N-labeled proteins. The CPD-HNCO experiment renders 50% sensitivity enhancement over the conventional CT-HNCO experiment performed on a 12 kDa FK506 binding protein, when a total of 266 ms of amide nitrogen-carbonyl carbon defocusing and refocusing periods is employed. This is a typical time period for the direct detection of hydrogen bonds in proteins via trans- hydrogen bond (3h)J(NC') couplings. The experimental data fit theoretical analysis well. The significant enhancement in sensitivity makes the experiment more applicable to larger-sized proteins without resorting to perdeuteration.
Keywords:	sensitivity and specificity; proteins; molecular dynamics; image enhancement; nuclear magnetic resonance spectroscopy; hydrogen bond; hydrogen bonding; molecular interaction; protein structure; m protein; nitrogen; carbon isotopes; nitrogen isotopes; hydrogen bonds; nuclear magnetic resonance, biomolecular; carbon 13; fk 506 binding protein; priority journal; article; j-coupling mediated relaxation; protein nmr; sensitivity enhancement
Journal Title:	Journal of Biomolecular NMR
Volume:	17
Issue:	1
ISSN:	0925-2738
Publisher:	Springer
Date Published:	2000-05-01
Start Page:	55
End Page:	61
Language:	English
DOI:	10.1023/a:1008340116418
PUBMED:	10909866
PROVIDER:	scopus
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-0033932719&partnerID=40&md5=22b35bb91df1dc1aeab7dae02cc73533
Notes:	Export Date: 18 November 2015 -- Source: Scopus

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