Mechanism of the Flavoprotein l-HydroxynicotineOxidase: Kinetic Mechanism, Substrate Specificity, Reaction Product,and Roles of Active-Site Residues
Mechanism of the Flavoprotein l-HydroxynicotineOxidase: Kinetic Mechanism, Substrate Specificity, Reaction Product,and Roles of Active-Site Residues
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01325/20160115/images/medium/bi-2015-01325p_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01325
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[NMR paper] NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines.
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Adv Exp Med Biol. 2015;870:49-122
Authors: Brutscher B, Felli IC, Gil-Caballero S, Hoek T, Kümmerle R, Piai A, Pierattelli R, Sólyom Z
Abstract
Thanks to recent improvements in NMR instrumentation, pulse sequence design, and...
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09-21-2015 03:01 PM
Erratic proteins: New insights into a transport mechanism - YottaFire
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YottaFire
â??Only through employing modern nuclear magnetic resonance spectroscopy, it has become possible to detect this dynamic behavior within Skp.â?? Transporting the membrane protein in such a changing state does not require energy and allows for its rapid ...
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Toronto NewsFIX
â??Only through employing modern nuclear magnetic resonance spectroscopy, it has become possible to detect this dynamic behavior within Skp.â?? Transporting the membrane protein in such a changing state does not require energy and allows for its rapid ...
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Erratic proteins: New insights into a transport mechanism - Phys.Org
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Erratic proteins: New insights into a transport mechanism
Phys.Org
"Only through employing modern nuclear magnetic resonance spectroscopy, it has become possible to detect this dynamic behavior within Skp." Transporting the membrane protein in such a changing state does not require energy and allows for its rapid ...
Erratic proteins: New insights into a transport mechanism - Phys.Org
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J Am Chem Soc. 2002 Apr 24;124(16):4522-34
Authors: Prompers JJ, Brüschweiler R
A general framework is presented for the interpretation of NMR relaxation data of proteins. The method, termed isotropic reorientational eigenmode dynamics (iRED), relies on a principal component...
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Analysis of error propagation from NMR-derived internuclear distances into molecular structure of cyclo-pro-gly.
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J Magn Reson. 1998 Dec;135(2):454-65
Authors: Dzakula Z, Jurani? , DeRider ML, Westler WM, Macura S, Markley JL
Analytical expressions have been derived that translate uncertainties in distance constraints (obtained from NMR investigations) into uncertainties in atom positions in the maximum likelihood...
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J Biomol NMR. 1993 Mar;3(2):225-31
Authors: Logan TM, Olejniczak ET, Xu RX, Fesik SW
A general approach for assigning the resonances of uniformly 15N- and 13C-labeled proteins in their unfolded state is presented. The assignment approach takes advantage of the spectral dispersion of the amide...