Computer model may help scientists split up, reassemble proteins on command - Phys.org
Computer model may help scientists split up, reassemble proteins on command - Phys.org
Computer model may help scientists split up, reassemble proteins on command Phys.orgSplitting up and getting back together is always hard to do, but for proteins, it's almost impossible.
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[NMR paper] Intrinsic Allosteric Inhibition of Signaling Proteins by Targeting Rare Interaction States Detected by High-Pressure NMR Spectroscopy.
Intrinsic Allosteric Inhibition of Signaling Proteins by Targeting Rare Interaction States Detected by High-Pressure NMR Spectroscopy.
Related Articles Intrinsic Allosteric Inhibition of Signaling Proteins by Targeting Rare Interaction States Detected by High-Pressure NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Nov 11;
Authors: Kalbitzer HR, Rosnizeck IC, Munte CE, Narayanan SP, Kropf V, Spoerner M
Abstract
A new type of allosteric inhibition by small molecules is proposed that should be applicable to all proteins involved intrinsically...
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11-13-2013 09:22 PM
[NMR paper] Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Related Articles Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Chembiochem. 2013 Jun 28;
Authors: Roche J, Ying J, Maltsev AS, Bax A
Abstract
The impact of pressure on the backbone (15) N, (1) H and (13) C chemical shifts in N-terminally acetylated ?-synuclein has been evaluated over a pressure range 1-2500 bar. Even while the chemical shifts fall very close...
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A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A
A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A
22 February 2012
Publication year: 2012
Source:Biophysical Journal, Volume 102, Issue 4</br>
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Outer surface protein A (OspA) is a crucial protein in the infection of Borrelia burgdorferi causing Lyme disease. We studied conformational fluctuations of OspA with high-pressure 15N/1H two-dimensional NMR along with high-pressure fluorescence spectroscopy. We found evidence within folded, native OspA for rapid local fluctuations of the...
Scientists use high pressure NMR spectroscopy to study structure of dynamic proteins - Phys.org
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