PAF and related antifungal proteins are promising antimicrobial agents. They have highly stable folds around room temperature due to the presence of 3-4 disulfide bonds. However, unfolded states persist and contribute to the thermal equilibrium in aqueous solution, and low-populated states might influence their biological impact. To explore such equilibria during dimethyl sulfoxide (DMSO)-induced chemical unfolding, we studied PAF and its inactive variant PAF^(D19S) using nuclear magnetic...
[NMR paper] 19F-NMR Unveils the Ligand-Induced Conformation of a Catalytically Inactive Twisted Homodimer of tRNA-Guanine Transglycosylase
19F-NMR Unveils the Ligand-Induced Conformation of a Catalytically Inactive Twisted Homodimer of tRNA-Guanine Transglycosylase
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...
Disulfide Bond Pattern of Transforming Growth Factor ?-Induced Protein
Disulfide Bond Pattern of Transforming Growth Factor ?-Induced Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00694/20160922/images/medium/bi-2016-006945_0011.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00694
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[NMR paper] Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.
Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.
Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.
Proc Natl Acad Sci U S A. 2016 Jul 11;
Authors: Huang R, Ripstein ZA, Augustyniak R, Lazniewski M, Ginalski K, Kay LE, Rubinstein JL
Abstract
The AAA+ (ATPases associated with a variety of cellular activities) enzymes play critical roles in a variety of homeostatic processes in all kingdoms of life. Valosin-containing protein-like ATPase of...
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07-13-2016 10:14 AM
[NMR paper] Combined ligand-observe (19)F and protein-observe (15)N,(1)H-HSQC NMR suggests phenylalanine as the key ?-somatostatin residue recognized by human protein disulfide isomerase.
Combined ligand-observe (19)F and protein-observe (15)N,(1)H-HSQC NMR suggests phenylalanine as the key ?-somatostatin residue recognized by human protein disulfide isomerase.
Combined ligand-observe (19)F and protein-observe (15)N,(1)H-HSQC NMR suggests phenylalanine as the key ?-somatostatin residue recognized by human protein disulfide isomerase.
Sci Rep. 2016;6:19518
Authors: Richards KL, Rowe ML, Hudson PB, Williamson RA, Howard MJ
Abstract
Human protein disulphide isomerase (hPDI) is an endoplasmic reticulum (ER) based...
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01-21-2016 01:08 PM
[NMR paper] "Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.
"Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.
Related Articles "Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.
Chemistry. 2015 Feb 12;
Authors: Fizil Á, Gáspári Z, Barna T, Marx F, Batta G
Abstract
Transition between conformational states in proteins is being recognized as a possible key factor...
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Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant
Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant
September 2012
Publication year: 2012
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes, Volume 1818, Issue 9</br>
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Membrane proteins are vital for biological function, and their action is governed by structural properties critically depending on their interactions with the membranes. This has motivated considerable interest in studies of membrane protein folding and unfolding. Here the structural changes...
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02-03-2013 10:13 AM
[NMR paper] High-resolution NMR study of the pressure-induced unfolding of lysozyme.
High-resolution NMR study of the pressure-induced unfolding of lysozyme.
Related Articles High-resolution NMR study of the pressure-induced unfolding of lysozyme.
Biochemistry. 1992 Sep 1;31(34):7773-8
Authors: Samarasinghe SD, Campbell DM, Jonas A, Jonas J
The pressure-induced reversible unfolding of lysozyme was investigated by high-resolution proton magnetic resonance spectroscopy by following the proton spectra of the following residues: His-15 epsilon 1, Trp-28 epsilon 3, Leu-17 delta 2, Cys-64 alpha, and Trp-108 epsilon 3. The...
DMSO-Induced Unfolding of the Antifungal Disulfide Protein PAF and Its Inactive Variant: A Combined NMR and DSC Study
Linear Mode
