Understanding the structural arrangements of protein oligomers can support the design of ligands that interfere with their function in order to develop new therapeutic concepts for disease treatment. Recent crystallographic studies have elucidated a novel twisted and functionally inactive form of the homodimeric enzyme tRNA-guanine transglycosylase (TGT), a putative target in the fight against shigellosis. Active-site ligands have been identified that stimulate the rearrangement of one monomeric...
[NMR paper] Phosphorylation-induced conformation of ?2-adrenoceptor related to arrestin recruitment revealed by NMR.
Phosphorylation-induced conformation of ?2-adrenoceptor related to arrestin recruitment revealed by NMR.
Related Articles Phosphorylation-induced conformation of ?2-adrenoceptor related to arrestin recruitment revealed by NMR.
Nat Commun. 2018 Jan 15;9(1):194
Authors: Shiraishi Y, Natsume M, Kofuku Y, Imai S, Nakata K, Mizukoshi T, Ueda T, Iwaï H, Shimada I
Abstract
The C-terminal region of G-protein-coupled receptors (GPCRs), stimulated by agonist binding, is phosphorylated by GPCR kinases, and the phosphorylated GPCRs bind to...
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01-18-2018 12:41 PM
Using Ligand-Induced Protein Chemical Shift PerturbationsTo Determine Protein–Ligand Structures
Using Ligand-Induced Protein Chemical Shift PerturbationsTo Determine Protein–Ligand Structures
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00170/20170427/images/medium/bi-2017-001707_0012.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00170
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/BrFG2OzcmDE
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Do twisted laser beams evoke nuclear hyperpolarization?
From The DNP-NMR Blog:
Do twisted laser beams evoke nuclear hyperpolarization?
Schmidt, A.B., et al., Do twisted laser beams evoke nuclear hyperpolarization? J Magn Reson, 2016. 268: p. 58-67.
http://www.ncbi.nlm.nih.gov/pubmed/27179228
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07-20-2016 10:59 PM
[NMR paper] CORCEMA refinement of the bound ligand conformation within the protein binding pocket
CORCEMA refinement of the bound ligand conformation within the protein binding pocket in reversibly forming weak complexes using STD-NMR intensities.
Related Articles CORCEMA refinement of the bound ligand conformation within the protein binding pocket in reversibly forming weak complexes using STD-NMR intensities.
J Magn Reson. 2004 May;168(1):36-45
Authors: Jayalakshmi V, Rama Krishna N
We describe an intensity-restrained optimization procedure for refining approximate structures of ligands within the protein binding pockets using STD-NMR...
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11-24-2010 09:51 PM
[NMR paper] Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation o
Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation of Asp 85 and deprotonation of Schiff base as studied by 13C NMR.
Related Articles Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation of Asp 85 and deprotonation of Schiff base as studied by 13C NMR.
Biochemistry. 2000 Nov 28;39(47):14472-80
Authors: Kawase Y, Tanio M, Kira A, Yamaguchi S, Tuzi S, Naito A, Kataoka M, Lanyi JK, Needleman R, Saitô H
According to previous X-ray diffraction studies, the D85N mutant of...
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11-19-2010 08:29 PM
[NMR paper] 31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes
31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes.
Related Articles 31P NMR analysis of the DNA conformation induced by protein binding SRY/DNA complexes.
Eur J Biochem. 2000 Feb;267(4):1223-9
Authors: Castagné C, Murphy EC, Gronenborn AM, Delepierre M
Complexes of the HMG box protein SRY with two duplexes of 8 and 14 base pairs have been studied by 31P NMR and complete assignment of all phosphorus signals of the bound DNA duplexes are presented. While for the free DNA, all 31P signals display limited...
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11-18-2010 09:15 PM
[NMR paper] NMR spectroscopic analysis of the DNA conformation induced by the human testis determ
NMR spectroscopic analysis of the DNA conformation induced by the human testis determining factor SRY.
Related Articles NMR spectroscopic analysis of the DNA conformation induced by the human testis determining factor SRY.
Biochemistry. 1995 Sep 19;34(37):11998-2004
Authors: Werner MH, Bianchi ME, Gronenborn AM, Clore GM
The conformation of an eight base pair DNA oligonucleotide duplex bound to the human testis determining factor SRY and the orientation of the protein domain within the complex have been analyzed by a variety of NMR methods...
19F-NMR Unveils the Ligand-Induced Conformation of a Catalytically Inactive Twisted Homodimer of tRNA-Guanine Transglycosylase
Linear Mode
