ModA is a soluble periplasmic molybdate-binding protein found in most gram-negative bacteria. It is part of the ABC transporter complex ModABC that moves molybdenum into the cytoplasm, to be used by enzymes that carry out various redox reactions. Since there is no clear analog for ModA in humans, this protein could be a good target for antibacterial drug design. Backbone ¹H, ^(13)C and ^(15)N chemical shifts of apo and molybdate-bound ModA from E. coli were assigned at pHs 6.0 and 4.5. In...
[NMR paper] Solid-state NMR chemical shift analysis for determining the conformation of ATP bound to Na,K-ATPase in its native membrane
Solid-state NMR chemical shift analysis for determining the conformation of ATP bound to Na,K-ATPase in its native membrane
Structures of membrane proteins determined by X-ray crystallography and, increasingly, by cryo-electron microscopy often fail to resolve the structural details of unstable or reactive small molecular ligands in their physiological sites. This work demonstrates that ^(13)C chemical shifts measured by magic-angle spinning (MAS) solid-state NMR (SSNMR) provide unique information on the conformation of a labile ligand in the physiological site of a functional protein in...
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[NMR paper] Chemical shift transfer: an effective strategy for protein NMR assignment with ARTINA
Chemical shift transfer: an effective strategy for protein NMR assignment with ARTINA
Chemical shift transfer (CST) is a well-established technique in NMR spectroscopy that utilizes the chemical shift assignment of one protein (source) to identify chemical shifts of another (target). Given similarity between source and target systems (e.g., using homologs), CST allows the chemical shifts of the target system to be assigned using a limited amount of experimental data. In this study, we propose a deep-learning based workflow, ARTINA-CST, that automates this procedure, allowing CST...
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[NMR paper] Correction to: Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid.
Correction to: Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Correction to: Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid.
Biomol NMR Assign. 2019 Apr 02;:
Authors: Jones DNM, Wang J, Murphy EJ
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04-05-2019 08:33 AM
[NMR paper] Backbone (1)H, (15)N, (13)C and side chain (13)C? NMR chemical shift assignment of murine interleukin-10.
Backbone (1)H, (15)N, (13)C and side chain (13)C? NMR chemical shift assignment of murine interleukin-10.
Backbone (1)H, (15)N, (13)C and side chain (13)C? NMR chemical shift assignment of murine interleukin-10.
Biomol NMR Assign. 2013 Aug 25;
Authors: Künze G, Theisgen S, Huster D
Abstract
Almost complete assignment of backbone (1)H, (13)C, (15)N and side chain (13)C? resonances for the immune-regulatory cytokine IL-10 is reported. The protein was overexpressed in Escherichia coli and was refolded from inclusion bodies. The point...
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08-29-2013 01:53 PM
[NMR paper] Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information.
Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information.
Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information.
J Biomol NMR. 2013 Apr 28;
Authors: Fritzsching KJ, Yang Y, Schmidt-Rohr K, Hong M
Abstract
We introduce a Python-based program that utilizes the large database of (13)C and (15)N chemical shifts in the Biological Magnetic...
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04-30-2013 10:21 PM
[NMR paper] Selective chemical shift assignment of B800 and B850 bacteriochlorophylls in uniforml
Selective chemical shift assignment of B800 and B850 bacteriochlorophylls in uniformly -labeled light-harvesting complexes by solid-state NMR spectroscopy at ultra-high magnetic field.
Related Articles Selective chemical shift assignment of B800 and B850 bacteriochlorophylls in uniformly -labeled light-harvesting complexes by solid-state NMR spectroscopy at ultra-high magnetic field.
J Am Chem Soc. 2005 Mar 9;127(9):3213-9
Authors: van Gammeren AJ, Buda F, Hulsbergen FB, Kiihne S, Hollander JG, Egorova-Zachernyuk TA, Fraser NJ, Cogdell RJ, de Groot HJ
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11-24-2010 11:14 PM
[NMR paper] Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignment
Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignments and secondary structure of malate synthase g.
Related Articles Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignments and secondary structure of malate synthase g.
J Am Chem Soc. 2002 Aug 28;124(34):10025-35
Authors: Tugarinov V, Muhandiram R, Ayed A, Kay LE
A four-dimensional (4-D) NMR study of Escherichia coli malate synthase G (MSG), a 723-residue monomeric enzyme (81.4 kDa), is described. Virtually complete backbone (1)HN,...
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11-24-2010 08:58 PM
[NMR paper] The chemical shift index: a fast and simple method for the assignment of protein seco
The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.
Related Articles The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.
Biochemistry. 1992 Feb 18;31(6):1647-51
Authors: Wishart DS, Sykes BD, Richards FM
Previous studies by Wishart et al. have demonstrated that 1H NMR chemical shifts are strongly dependent on the character and nature of protein secondary structure. In particular, it has been...
Solution NMR chemical shift assignment of apo and molybdate-bound ModA at two pHs
Linear Mode
