Literature DB >> 12932470

15N chemical shift anisotropy in protein structure refinement and comparison with NH residual dipolar couplings.

Rebecca S Lipsitz1, Nico Tjandra.   

Abstract

Recent methods of aligning proteins which were developed in order to measure residual dipolar couplings (RDCs) in solution can also be used for additional applications such as measuring the 15N CSA in the form of chemical shift differences, Deltadelta. A new XPLOR-NIH module has been developed and implemented for NMR structure refinement using the 15N Deltadelta data as restraints. The results of this refinement are shown using the protein Bax. This method should be amenable to any protein which can be studied by NMR. An analysis comparing the structural information provided by NH RDCs and the 15N Deltadelta is included.

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Year:  2003        PMID： 12932470     DOI： 10.1016/s1090-7807(03)00176-9

Source DB:  PubMed          Journal:  J Magn Reson        ISSN： 1090-7807            Impact factor:   2.229


  21 in total

Review 1.  Structure determination of membrane proteins by NMR spectroscopy.

Authors:  Stanley J Opella; Francesca M Marassi
Journal:  Chem Rev       Date:  2004-08       Impact factor: 60.622

2.  Structure and dynamics of the membrane-bound form of Pf1 coat protein: implications of structural rearrangement for virus assembly.

Authors:  Sang Ho Park; Francesca M Marassi; David Black; Stanley J Opella
Journal:  Biophys J       Date:  2010-09-08       Impact factor: 4.033

Review 3.  The use of residual dipolar coupling in studying proteins by NMR.

Authors:  Kang Chen; Nico Tjandra
Journal:  Top Curr Chem       Date:  2012

4.  Variability of the 15N chemical shielding tensors in the B3 domain of protein G from 15N relaxation measurements at several fields. Implications for backbone order parameters.

Authors:  Jennifer B Hall; David Fushman
Journal:  J Am Chem Soc       Date:  2006-06-21       Impact factor: 15.419

5.  Refinement of protein structure against non-redundant carbonyl 13C NMR relaxation.

Authors:  Nico Tjandra; Motoshi Suzuki; Shou-Lin Chang
Journal:  J Biomol NMR       Date:  2007-06-07       Impact factor: 2.835

6.  Top-down approach in protein RDC data analysis: de novo estimation of the alignment tensor.

Authors:  Kang Chen; Nico Tjandra
Journal:  J Biomol NMR       Date:  2007-06-26       Impact factor: 2.835

7.  Orientation of the Escherichia coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-State NMR.

Authors:  Radhakrishnan Mahalakshmi; Francesca M Marassi
Journal:  Biochemistry       Date:  2008-06-24       Impact factor: 3.162

8.  AssignFit: a program for simultaneous assignment and structure refinement from solid-state NMR spectra.

Authors:  Ye Tian; Charles D Schwieters; Stanley J Opella; Francesca M Marassi
Journal:  J Magn Reson       Date:  2011-10-08       Impact factor: 2.229

9.  Residual dipolar coupling measurements of transmembrane proteins using aligned low-q bicelles and high-resolution magic angle spinning NMR spectroscopy.

Authors:  Christian G Canlas; Dejian Ma; Pei Tang; Yan Xu
Journal:  J Am Chem Soc       Date:  2008-09-13       Impact factor: 15.419

10.  Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic ¹⁵N chemical shielding anisotropy tensors.

Authors:  Jiří Emmer; Andrea Vavrinská; Vladimír Sychrovský; Ladislav Benda; Zdeněk Kříž; Jaroslav Koča; Rolf Boelens; Vladimír Sklenář; Lukáš Trantírek
Journal:  J Biomol NMR       Date:  2012-12-01       Impact factor: 2.835
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