Tryptophan plays a critical role in proteins by contributing to stability, allostery, and catalysis. Using fluorine (^(19)F) nuclear magnetic resonance (NMR), protein conformational dynamics and structure-activity relationships (SARs) can be studied via fluorotryptophan reporters. Tryptophan analogs such as 4-, 5-, 6-, or 7-fluorotryptophan can be routinely incorporated into proteins during heterologous expression by arresting endogenous tryptophan biosynthesis. Building upon the large ^(19)F...
[NMR paper] Conformational exchange of the Zalpha domain of human RNA editing enzyme ADAR1 studied by NMR spectroscopy
Conformational exchange of the Zalpha domain of human RNA editing enzyme ADAR1 studied by NMR spectroscopy
Z-DNA binding proteins (ZBPs) play important roles in RNA editing, innate immune responses, and viral infections. Numerous studies have implicated a role for conformational motions during ZBPs binding upon DNA, but the quantitative intrinsic conformational exchanges of ZBP have not been elucidated. To understand the correlation between the biological function and dynamic feature of the Z? domains of human ADAR1 (hZ?(ADAR1)), we have performed the ^(15)N backbone amide...
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10-09-2021 06:32 PM
[NMR paper] Biophysical characterization and a roadmap towards the NMR solution structure of G0S2, a key enzyme in non-alcoholic fatty liver disease
Biophysical characterization and a roadmap towards the NMR solution structure of G0S2, a key enzyme in non-alcoholic fatty liver disease
In the United States non-alcoholic fatty liver disease (NAFLD) is the most common form of chronic liver disease, affecting an estimated 80 to 100 million people. It occurs in every age group, but predominantly in people with risk factors such as obesity and type 2 diabetes. NAFLD is marked by fat accumulation in the liver leading to liver inflammation, which may lead to scarring and irreversible damage progressing to cirrhosis and liver failure. In animal...
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07-15-2021 03:56 PM
[ASAP] Enzyme-Directed Functionalization of Designed, Two-Dimensional Protein Lattices
Enzyme-Directed Functionalization of Designed, Two-Dimensional Protein Lattices
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00363/20200803/images/medium/bi0c00363_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00363
http://feeds.feedburner.com/~r/acs/bichaw/~4/5SDEU5qpzmk
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08-04-2020 12:56 PM
[NMR paper] A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.
A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.
Related Articles A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.
Chem Commun (Camb). 2015 Nov 10;
Authors: Mallagaray A, Domínguez G, Peters T, Pérez-Castells J
Abstract
Attachment of human noroviruses to histo blood group antigens is thought to be essential for infection of host cells. Molecular details of the attachment process can be studied in vitro using a...
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11-11-2015 02:40 PM
[NMR paper] Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering.
Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering.
Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering.
Proc Natl Acad Sci U S A. 2015 Aug 24;
Authors: Venditti V, Schwieters CD, Grishaev A, Clore GM
Abstract
Enzyme I (EI) is the first component in the bacterial phosphotransferase system, a signal transduction pathway in which phosphoryl transfer through a series...
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08-26-2015 10:21 AM
[NMR paper] Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy.
Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy.
Related Articles Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy.
Proteins. 2014 Jul 26;
Authors: Gupta S, Bhattacharjya S
Abstract
The sterile alpha motif or SAM domain is one of the most frequently present protein interaction modules with diverse functional attributions. SAM domain of the Ste11 protein of budding yeast plays important roles in...
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07-30-2014 10:22 AM
[NMR paper] Evolution of the concept of conformational dynamics of enzyme functions over half of a century: A personal view.
Evolution of the concept of conformational dynamics of enzyme functions over half of a century: A personal view.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Evolution of the concept of conformational dynamics of enzyme functions over half of a century: A personal view.
Biopolymers. 2013 Apr;99(4):263-9
Authors: Závodszky P, Hajdú I
Abstract
To most physicists, it was always evident that conformational fluctuation is an inherent...
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02-03-2013 10:19 AM
Influence of 1H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins
Influence of 1H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Yi-Jan Lin, Donata K. Kirchner, Peter Güntert</br>
Homodimeric proteins pose a difficulty for NMR structure determination because the degeneracy of the chemical shifts in the two identical monomers implies an ambiguity in all assignments of distance restraints. For homodimeric proteins, residues involved in the interface between two monomers provide essential intermolecular NOEs. The...
Characterization of conformational states of the homodimeric enzyme fluoroacetate dehalogenase by (19)F-(13)C two-dimensional NMR
Linear Mode
