What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein - Nature.com
What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein - Nature.com
What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein - Nature.com
[NMR paper] The precious fluorine on the ring: fluorine NMR for biological systems.
The precious fluorine on the ring: fluorine NMR for biological systems.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles The precious fluorine on the ring: fluorine NMR for biological systems.
J Biomol NMR. 2020 Jul 10;:
Authors: Boeszoermenyi A, Ogórek B, Jain A, Arthanari H, Wagner G
Abstract
The fluorine-19 nucleus was recognized early to harbor exceptional properties for NMR spectroscopy. With 100% natural abundance, a high...
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07-13-2020 01:56 AM
The precious fluorine on the ring: fluorine NMR for biological systems
The precious fluorine on the ring: fluorine NMR for biological systems
Abstract
The fluorine-19 nucleus was recognized early to harbor exceptional properties for NMR spectroscopy. With 100% natural abundance, a high gyromagnetic ratio (83% sensitivity compared to 1H), a chemical shift that is extremely sensitive to its surroundings and near total absence in biological systems, it was destined to become a favored NMR probe, decorating small and large molecules. However, after early excitement, where uptake of fluorinated aromatic amino acids was...
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07-10-2020 08:40 PM
[NMR paper] Cold-Shock Expression System in E. coli for Protein NMR Studies.
Cold-Shock Expression System in E. coli for Protein NMR Studies.
Related Articles Cold-Shock Expression System in E. coli for Protein NMR Studies.
Methods Mol Biol. 2017;1586:345-357
Authors: Sugiki T, Fujiwara T, Kojima C
Abstract
The cold-shock system using the pCold vector is one of the most effective Escherichia coli heterologous protein expression systems. It allows the improvement of the expression level of the protein of interest in a soluble fraction. In this chapter, we describe practical procedures for the...
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[NMR paper] Weak Intermolecular Hydrogen Bonds with Fluorine: Detection and Implications for Enzymatic/Chemical Reactions, Chemical Properties, and Ligand/Protein Fluorine NMR Screening.
Weak Intermolecular Hydrogen Bonds with Fluorine: Detection and Implications for Enzymatic/Chemical Reactions, Chemical Properties, and Ligand/Protein Fluorine NMR Screening.
Related Articles Weak Intermolecular Hydrogen Bonds with Fluorine: Detection and Implications for Enzymatic/Chemical Reactions, Chemical Properties, and Ligand/Protein Fluorine NMR Screening.
Chemistry. 2016 Apr 26;
Authors: Dalvit C, Vulpetti A
Abstract
It is known that strong hydrogen-bonding interactions play an important role in many chemical and...
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04-27-2016 01:51 PM
[NMR paper] (19)F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b'x from human protein disulphide isomerase (hPDI).
(19)F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b'x from human protein disulphide isomerase (hPDI).
Related Articles (19)F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b'x from human protein disulphide isomerase (hPDI).
Org Biomol Chem. 2014 May 6;
Authors: Curtis-Marof R, Doko D, Rowe ML, Richards KL, Williamson RA, Howard MJ
Abstract
We report a protein-observe (19)F NMR-based ligand titration binding study of human PDI b'x with ?-somatostatin that also emphasises...
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05-08-2014 05:26 AM
[NMR images] cspa is the major cold shock protein of the bacterial
http://www-nmr.cabm.rutgers.edu/photogallery/proteins/gif/3MEF-v3b.jpg
20/03/2014 12:45:23 PM GMT
cspa is the major cold shock protein of the bacterial
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03-20-2014 12:44 PM
[NMR paper] NMR of hydrogen bonding in cold-shock protein A and an analysis of the influence of c
NMR of hydrogen bonding in cold-shock protein A and an analysis of the influence of crystallographic resolution on comparisons of hydrogen bond lengths.
Related Articles NMR of hydrogen bonding in cold-shock protein A and an analysis of the influence of crystallographic resolution on comparisons of hydrogen bond lengths.
Protein Sci. 2001 Sep;10(9):1856-68
Authors: Alexandrescu AT, Snyder DR, Abildgaard F
Hydrogen bonding in cold-shock protein A of Escherichia coli has been investigated using long-range HNCO spectroscopy. Nearly half of the...
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11-19-2010 08:44 PM
[NMR paper] NMR assignments for acid-denatured cold shock protein A.
NMR assignments for acid-denatured cold shock protein A.
Related Articles NMR assignments for acid-denatured cold shock protein A.
J Biomol NMR. 1998 May;11(4):461-2
Authors: Alexandrescu AT, Rathgeb-Szabo K