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 conjugates, however, the effect of local environment vicinal to the protein ligation site on the paramagnetic effects remains poorly understood. In the present work, the stereospecific effect of chiral tether between the protein and a tag on the paramagnetic effects produced by the tag attached via a D- and L-type linker between the protein and paramagnetic metal chelating moiety was assessed. The remarkable chiral effect of the D- and L-type tether between the tag and the protein on the rigidity of paramagnetic tag is disclosed in a number of protein-tag-Ln complexes. The chiral tether formed between the D-type tag and L-type protein surface minimizes the effect of the local environment surrounding the ligation site on the averaging of paramagnetic tag, which is helpful to preserve the rigidity of a paramagnetic tag in the protein conjugates.
[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...
nmrlearner
Journal club
0
04-27-2018 05:00 AM
[NMR paper] Short two-armed lanthanide-binding tags for paramagnetic NMR spectroscopy based on chiral 1,4,7,10-tetrakis(2-hydroxypropyl)-1,4,7,10-tetraazacyclododecane scaffolds.
Short two-armed lanthanide-binding tags for paramagnetic NMR spectroscopy based on chiral 1,4,7,10-tetrakis(2-hydroxypropyl)-1,4,7,10-tetraazacyclododecane scaffolds.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Short two-armed lanthanide-binding tags for paramagnetic NMR spectroscopy based on chiral 1,4,7,10-tetrakis(2-hydroxypropyl)-1,4,7,10-tetraazacyclododecane scaffolds.
Chem Commun (Camb). 2017 Nov 22;:
Authors: Lee MD, Dennis ML, Graham B, Swarbrick JD
...
nmrlearner
Journal club
0
11-24-2017 04:57 AM
The DEAD-Box Protein CYT-19 Uses Arginine Residuesin Its C-Tail To Tether RNA Substrates
The DEAD-Box Protein CYT-19 Uses Arginine Residuesin Its C-Tail To Tether RNA Substrates
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00362/20170707/images/medium/bi-2017-00362h_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00362
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/zo-Bg-q4qiA
More...
nmrlearner
Journal club
0
07-08-2017 02:54 PM
[NMR paper] Chiral discrimination of ?-hydroxy acids and N-Ts-?-amino acids induced by tetraaza macrocyclic chiral solvating agents by using (1)H NMR spectroscopy.
Chiral discrimination of ?-hydroxy acids and N-Ts-?-amino acids induced by tetraaza macrocyclic chiral solvating agents by using (1)H NMR spectroscopy.
Related Articles Chiral discrimination of ?-hydroxy acids and N-Ts-?-amino acids induced by tetraaza macrocyclic chiral solvating agents by using (1)H NMR spectroscopy.
Org Biomol Chem. 2017 Jan 27;:
Authors: Lv C, Feng L, Zhao H, Wang G, Stavropoulos P, Ai L
Abstract
In the field of chiral recognition, reported chiral discrimination by (1)H NMR spectroscopy has mainly focused on...
nmrlearner
Journal club
0
01-28-2017 08:29 PM
[NMR paper] Cyclic pentapeptides of chiral sequence DLDDL as scaffold for antagonism of G-protein
Cyclic pentapeptides of chiral sequence DLDDL as scaffold for antagonism of G-protein coupled receptors: synthesis, activity and conformational analysis by NMR and molecular dynamics of ITF 1565 a substance P inhibitor.
Related Articles Cyclic pentapeptides of chiral sequence DLDDL as scaffold for antagonism of G-protein coupled receptors: synthesis, activity and conformational analysis by NMR and molecular dynamics of ITF 1565 a substance P inhibitor.
Biopolymers. 1999 Aug;50(2):211-9
Authors: Porcelli M, Casu M, Lai A, Saba G, Pinori M, Cappelletti S,...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] Stereospecific assignments of the leucine methyl resonances in the 1H NMR spectrum of
Stereospecific assignments of the leucine methyl resonances in the 1H NMR spectrum of Lactobacillus casei dihydrofolate reductase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Stereospecific assignments of the leucine methyl resonances in the 1H NMR spectrum of Lactobacillus casei dihydrofolate reductase.
FEBS Lett. 1993 Mar 1;318(2):177-80
Authors: Ostler G, Soteriou A, Moody CM, Khan JA, Birdsall B, Carr MD, Young DW, Feeney J
A general method is described for the...