Literature DB >> 17310328

Improved magnetization alignment schemes for spin-lock relaxation experiments.

D Flemming Hansen1, Lewis E Kay.   

Abstract

A pair of pulse schemes that spin-lock magnetization efficiently are presented. The design of the sequences benefited from a particularly simple relation that is derived describing to first order the evolution of any magnetization component due to the application of an off-resonance 90 degrees pulse. The sequences are shown theoretically and experimentally to significantly outperform the 90 degrees -delay-90 degrees element that is often used in current applications. It is shown that alignment of magnetization to within 1 degrees of the effective field can be obtained over a bandwidth extending between [-omega(SL), omega(SL)], where omega(SL) is the strength of the spin-lock field using a simple scheme that is an order of magnitude shorter than an adiabatic pulse that might also be used for a similar purpose.

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Year:  2007        PMID: 17310328     DOI: 10.1007/s10858-006-9126-6

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN: 0925-2738            Impact factor:   2.835


  12 in total

1.  Applications of natural-abundance nitrogen-15 nuclear magnetic resonance to large biochemically important molecules.

Authors:  D Gust; R B Moon; J D Roberts
Journal:  Proc Natl Acad Sci U S A       Date:  1975-12       Impact factor: 11.205

Review 2.  Protein dynamics from NMR.

Authors:  R Ishima; D A Torchia
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3.  Off-resonance R1rho relaxation outside of the fast exchange limit: an experimental study of a cavity mutant of T4 lysozyme.

Authors:  Dmitry M Korzhnev; Vladislav Yu Orekhov; Frederick W Dahlquist; Lewis E Kay
Journal:  J Biomol NMR       Date:  2003-05       Impact factor: 2.835

4.  Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformation.

Authors:  Ariel A Di Nardo; Dmitry M Korzhnev; Peter J Stogios; Arash Zarrine-Afsar; Lewis E Kay; Alan R Davidson
Journal:  Proc Natl Acad Sci U S A       Date:  2004-05-17       Impact factor: 11.205

Review 5.  Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy.

Authors:  Arthur G Palmer; Francesca Massi
Journal:  Chem Rev       Date:  2006-05       Impact factor: 60.622

6.  An Off-resonance Rotating Frame Relaxation Experiment for the Investigation of Macromolecular Dynamics Using Adiabatic Rotations

Authors: 
Journal:  J Magn Reson       Date:  1998-04       Impact factor: 2.229

7.  Carbon-13 nuclear magnetic resonance relaxation studies of internal mobility of the polypeptide chain in basic pancreatic trypsin inhibitor and a selectively reduced analogue.

Authors:  R Richarz; K Nagayama; K Wüthrich
Journal:  Biochemistry       Date:  1980-11-11       Impact factor: 3.162

8.  Backbone dynamics of a model membrane protein: 13C NMR spectroscopy of alanine methyl groups in detergent-solubilized M13 coat protein.

Authors:  G D Henry; J H Weiner; B D Sykes
Journal:  Biochemistry       Date:  1986-02-11       Impact factor: 3.162

9.  Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease.

Authors:  L E Kay; D A Torchia; A Bax
Journal:  Biochemistry       Date:  1989-11-14       Impact factor: 3.162

10.  Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects.

Authors:  K L Maxwell; A R Davidson
Journal:  Biochemistry       Date:  1998-11-17       Impact factor: 3.162

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  9 in total

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Journal:  J Biomol NMR       Date:  2013-08-02       Impact factor: 2.835

2.  Fast-time scale dynamics of outer membrane protein A by extended model-free analysis of NMR relaxation data.

Authors:  Binyong Liang; Ashish Arora; Lukas K Tamm
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3.  Mathematical treatment of adiabatic fast passage pulses for the computation of nuclear spin relaxation rates in proteins with conformational exchange.

Authors:  Renate Auer; Martin Tollinger; Ilya Kuprov; Robert Konrat; Karin Kloiber
Journal:  J Biomol NMR       Date:  2011-09-27       Impact factor: 2.835

Review 4.  NMR Methods for Characterizing the Basic Side Chains of Proteins: Electrostatic Interactions, Hydrogen Bonds, and Conformational Dynamics.

Authors:  Dan Nguyen; Chuanying Chen; B Montgomery Pettitt; Junji Iwahara
Journal:  Methods Enzymol       Date:  2018-09-27       Impact factor: 1.600

5.  Measurement of ¹⁵N relaxation rates in perdeuterated proteins by TROSY-based methods.

Authors:  Nils-Alexander Lakomek; Jinfa Ying; Ad Bax
Journal:  J Biomol NMR       Date:  2012-06-12       Impact factor: 2.835

6.  Selective characterization of microsecond motions in proteins by NMR relaxation.

Authors:  D Flemming Hansen; Haniqiao Feng; Zheng Zhou; Yawen Bai; Lewis E Kay
Journal:  J Am Chem Soc       Date:  2009-11-11       Impact factor: 15.419

7.  CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions.

Authors:  Tairan Yuwen; Nikolai R Skrynnikov
Journal:  J Biomol NMR       Date:  2014-02-05       Impact factor: 2.835

8.  Detection of nanosecond time scale side-chain jumps in a protein dissolved in water/glycerol solvent.

Authors:  Jun Xu; Yi Xue; Nikolai R Skrynnikov
Journal:  J Biomol NMR       Date:  2009-07-07       Impact factor: 2.835

9.  A Unique and Simple Approach to Improve Sensitivity in 15N-NMR Relaxation Measurements for NH₃⁺ Groups: Application to a Protein-DNA Complex.

Authors:  Dan Nguyen; Ganesh L R Lokesh; David E Volk; Junji Iwahara
Journal:  Molecules       Date:  2017-08-15       Impact factor: 4.411

  9 in total

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