scholarly journals Conformational dynamics of recoverin's Ca2+ -myristoyl switch probed by 15 N NMR relaxation dispersion and chemical shift analysis

2011 ◽  
Vol 79 (6) ◽  
pp. 1910-1922 ◽  
Author(s):  
Xianzhong Xu ◽  
Rieko Ishima ◽  
James B. Ames
Keyword(s):  
Chemical Shift ◽  
Conformational Dynamics ◽  
Nmr Relaxation ◽  
Relaxation Dispersion ◽  
Shift Analysis ◽  
Chemical Shift Analysis ◽  
Myristoyl Switch

scholarly journals Characterizing the Microstructure of Heparin and Heparan Sulfate UsingN-Sulfoglucosamine1H and15N NMR Chemical Shift Analysis

2012 ◽  
Vol 85 (2) ◽  
pp. 1247-1255 ◽  
Author(s):  
Derek J. Langeslay ◽  
Consuelo N. Beecher ◽  
Annamaria Naggi ◽  
Marco Guerrini ◽  
Giangiacomo Torri ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Heparan Sulfate ◽  
Nmr Chemical Shift ◽  
Shift Analysis ◽  
Chemical Shift Analysis

Protein chemical shift analysis: a practical guide

1998 ◽  
Vol 76 (2-3) ◽  
pp. 153-163 ◽  
Author(s):  
David S Wishart ◽  
Alex M Nip
Keyword(s):  
Chemical Shift ◽  
Selection Criteria ◽  
Three Dimensional ◽  
Random Coil ◽  
Chemical Shift Prediction ◽  
Contour Maps ◽  
Shift Analysis ◽  
Protein Chemical Shift ◽  
Chemical Shift Analysis ◽  
Heteronuclear Chemical Shift

Proper protein chemical shift analysis requires careful experimental measurements and the implementation of standardized referencing procedures. In this article we outline the steps necessary to ensure proper chemical shift referencing and the selection criteria for choosing appropriate "random coil" amino acid chemical shift values for predicting, comparing, and assigning 1H, 13C, and 15N resonances in proteins. By making use of these standardized conditions we demonstrate how several recently developed methods, namely homologous assignment techniques and empirical chemical shift contour maps (or hypersurfaces), can significantly improve the accuracy of chemical shift prediction for 1H, 13C, and 15N nuclei. In addition to illustrating the potential utility of chemical shift prediction, we also outline procedures for identifying secondary structure elements through heteronuclear chemical shift analysis and further demonstrate how empirical shift contour maps can actually be used to refine, and more importantly generate, reasonably good three-dimensional protein structures.Key words: NMR, chemical shift, prediction, structure, protein.

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