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Gradient‐enhanced TROSY described with Cartesian product operators

dc.contributor.authorZuiderweg, Erik R. P.en_US
dc.contributor.authorRousaki, Aikaterinien_US
dc.date.accessioned2011-12-05T18:32:21Z
dc.date.available2013-01-02T16:32:42Zen_US
dc.date.issued2011-11en_US
dc.identifier.citationZuiderweg, Erik R.P.; Rousaki, Aikaterini (2011). "Gradient‐enhanced TROSY described with Cartesian product operators." Concepts in Magnetic Resonance Part A 38A(6): 280-288. <http://hdl.handle.net/2027.42/88024>en_US
dc.identifier.issn1546-6086en_US
dc.identifier.issn1552-5023en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/88024
dc.description.abstractTROSY, Transverse Relaxation Optimized Spectroscopy, was developed more than a decade ago. Since that time, the 15 N‐ 1 H HSQC‐TROSY experiment has become the standard “fingerprint” correlation spectrum for proteins of high molecular weight. In addition, its implementation in protein triple resonance experiments has pushed the boundaries of NMR assignment up to about 100 kDa, making NMR a highly relevant technique in structural biology. TROSY exploits the dipole‐CSA cross‐correlated relaxation properties of the NH system and selects for the narrowest of the HSQC J‐correlation quartet in both dimensions. The original publications and reviews of TROSY use shift operators and/or single transition product operators to describe the TROSY coherence pathways selections. In this review, we offer a familiar Cartesian product operator approach to comprehensively describe all of the events in the modern TROSY pulse sequence such as multiplet selection, gradient coherence selection, gradient quadrature, and sensitivity enhancement. © 2011 Wiley Periodicals, Inc. Concepts Magn Reson Part A 38: 280–288, 2011.en_US
dc.publisherWiley Subscription Services, Inc., A Wiley Companyen_US
dc.subject.otherProteinen_US
dc.subject.otherNMRen_US
dc.subject.otherCross‐Correlated Relaxationen_US
dc.titleGradient‐enhanced TROSY described with Cartesian product operatorsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelRadiologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, 1150 W. Medical Center Drive, Ann Arbor, MI 48109en_US
dc.contributor.affiliationumLSA Biophysics, University of Michigan, 930 N University Avenue, Ann Arbor, MI 48109en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, 1150 W. Medical Center Drive, Ann Arbor, MI 48109en_US
dc.contributor.affiliationotherInstitute of Organic Chemistry and Chemical Biology, Goethe University, Max‐von‐Laue‐Str. 7, Frankfurt, DE 60438en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/88024/1/20228_ftp.pdf
dc.identifier.doi10.1002/cmr.a.20228en_US
dc.identifier.sourceConcepts in Magnetic Resonance Part Aen_US
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dc.owningcollnameInterdisciplinary and Peer-Reviewed


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