[NMR paper] Protein interaction patterns in different cellular environments are revealed by in-cell NMR.
Protein interaction patterns in different cellular environments are revealed by in-cell NMR.
Related Articles Protein interaction patterns in different cellular environments are revealed by in-cell NMR.
Sci Rep. 2015;5:14456
Authors: Barbieri L, Luchinat E, Banci L
Abstract
In-cell NMR allows obtaining atomic-level information on biological macromolecules in their physiological environment. Soluble proteins may interact with the cellular environment in different ways: either specifically, with their functional partners, or...
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09-26-2015 05:13 AM
[NMR paper] Position and orientational preferences of drug-like compounds in lipid membranes: a computational and NMR approach.
Position and orientational preferences of drug-like compounds in lipid membranes: a computational and NMR approach.
Position and orientational preferences of drug-like compounds in lipid membranes: a computational and NMR approach.
Phys Chem Chem Phys. 2015 Jul 8;
Authors: Ma J, Domicevica L, Schnell JR, Biggin PC
Abstract
Permeation of drugs across lipid bilayers is a key factor in dictating how effective they will be. In vivo, the issue is compounded by the presence of drug-exporter proteins such as P-glycoprotein....
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR [Biophysics and Computational Biology]
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR
Kato, H., van Ingen, H., Zhou, B.-R., Feng, H., Bustin, M., Kay, L. E., Bai, Y....
Date: 2011-07-26
Chromatin structure and function are regulated by numerous proteins through specific binding to nucleosomes. The structural basis of many of these interactions is unknown, as in the case of the high mobility group nucleosomal (HMGN) protein family that regulates various chromatin functions, including transcription. Here, we report the architecture of the HMGN2-nucleosome...
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07-26-2011 11:22 PM
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy [Biophysics and Computational Biology]
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy
Masterson, L. R., Shi, L., Metcalfe, E., Gao, J., Taylor, S. S., Veglia, G....
Date: 2011-04-26
Protein kinase A (PKA) is a ubiquitous phosphoryl transferase that mediates hundreds of cell signaling events. During turnover, its catalytic subunit (PKA-C) interconverts between three major conformational states (open, intermediate, and closed) that are dynamically and allosterically activated by nucleotide binding. We show that the structural transitions between these...
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04-27-2011 04:16 AM
Solid-State 91Zr NMR Spectroscopy Studies of Zirconocene Olefin Polymerization Catalyst Precursors
Solid-State 91Zr NMR Spectroscopy Studies of Zirconocene Olefin Polymerization Catalyst Precursors
Aaron J. Rossini, Ivan Hung, Samuel A. Johnson, Carla Slebodnick, Mike Mensch, Paul A. Deck and Robert W. Schurko
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107749b/aop/images/medium/ja-2010-07749b_0012.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107749b
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/GGw8Igo70Jo
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12-03-2010 08:52 PM
[NMR paper] Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the
Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
Related Articles Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
J Biol Chem. 2000 Oct 13;275(41):31908-13
Authors: Macdonald JM, Haas AL, London RE
Reactivity of surface lysyl residues of proteins with a broad range of chemical agents has been proposed to be dependent on the catalytic microenvironment of the residue. We have investigated the acetylation of wild type...
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11-19-2010 08:29 PM
NMR spectroscopy and computational analysis of interaction between Serratia marcescen
NMR spectroscopy and computational analysis of interaction between Serratia marcescens chitinase B and a dipeptide derived from natural-product cyclopentapeptide chitinase inhibitor argifin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR spectroscopy and computational analysis of interaction between Serratia marcescens chitinase B and a dipeptide derived from natural-product cyclopentapeptide chitinase inhibitor argifin.
Bioorg Med Chem. 2010 Aug 15;18(16):5835-5844
Authors: ...
Remote-Stereocontrol in Dienamine Catalysis: Z-Dienamine Preferences and Electrophile–Catalyst Interaction Revealed by NMR and Computational Studies
Linear Mode
