Distinct stereospecific effect of chiral tether between a tag and protein on the rigidity of paramagnetic tag
Distinct stereospecific effect of chiral tether between a tag and protein on the rigidity of paramagnetic tag
Abstract
Flexibility between the paramagnetic tag and its protein conjugates is a common yet unresolved issue in the applications of paramagnetic NMR spectroscopy in biological systems. The flexibility greatly attenuates the magnetic anisotropy and compromises paramagnetic effects especially for pseudocontact shift and residual dipolar couplings. Great efforts have been made to improve the rigidity of paramagnetic tag in the protein...
[NMR paper] Dynamic Exchange of the Metal Chelating Moiety: A Key Factor in Determining the Rigidity of Protein-Tag Conjugates in Paramagnetic NMR.
Dynamic Exchange of the Metal Chelating Moiety: A Key Factor in Determining the Rigidity of Protein-Tag Conjugates in Paramagnetic NMR.
Dynamic Exchange of the Metal Chelating Moiety: A Key Factor in Determining the Rigidity of Protein-Tag Conjugates in Paramagnetic NMR.
J Phys Chem Lett. 2020 Oct 27;:9493-9500
Authors: Chen JL, Li B, Li XY, Su XC
Abstract
Site-specific labeling of proteins with a paramagnetic tag is an efficient way to provide atomic-resolution information about the dynamics, interactions, and structures of the...
nmrlearner
Journal club
0
10-28-2020 12:41 PM
Minimal NMR distance information for rigidity of protein graphs
Minimal NMR distance information for rigidity of protein graphs
Publication date: Available online 26 April 2018
Source:Discrete Applied Mathematics</br>
Author(s): Carlile Lavor, Leo Liberti, Bruce Donald, Bradley Worley, Benjamin Bardiaux, Thérèse E. Malliavin, Michael Nilges</br>
Nuclear Magnetic Resonance (NMR) experiments provide distances between nearby atoms of a protein molecule. The corresponding structure determination problem is to determine the 3D protein structure by exploiting such distances. We present a new order on the atoms of the...