[NMR paper] Weak and Transient Protein Interactions Determined by Solid-State NMR.
Weak and Transient Protein Interactions Determined by Solid-State NMR.
Related Articles Weak and Transient Protein Interactions Determined by Solid-State NMR.
Angew Chem Int Ed Engl. 2016 Apr 21;
Authors: Dannatt HR, Felletti M, Jehle S, Wang Y, Emsley L, Dixon NE, Lesage A, Pintacuda G
Abstract
Despite their roles in controlling many cellular processes, weak and transient interactions between large structured macromolecules and disordered protein segments cannot currently be characterized at atomic resolution by X-ray...
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[NMR paper] Examining weak protein-protein interactions in start codon recognition via NMR spectroscopy.
Examining weak protein-protein interactions in start codon recognition via NMR spectroscopy.
Examining weak protein-protein interactions in start codon recognition via NMR spectroscopy.
FEBS J. 2013 Nov 30;
Authors: Luna RE, Akabayov SR, Ziarek JJ, Wagner G
Abstract
Weak protein-protein interactions are critical in numerous biological processes. Unfortunately, they are difficult to characterize due to the high concentrations required for the production and detection of the complex population. The inherent sensitivity of NMR...
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[NMR paper] (19) F NMR Spectroscopy as a Probe of Cytoplasmic Viscosity and Weak Protein Interactions in Living Cells.
(19) F NMR Spectroscopy as a Probe of Cytoplasmic Viscosity and Weak Protein Interactions in Living Cells.
(19) F NMR Spectroscopy as a Probe of Cytoplasmic Viscosity and Weak Protein Interactions in Living Cells.
Chemistry. 2013 Aug 6;
Authors: Ye Y, Liu X, Zhang Z, Wu Q, Jiang B, Jiang L, Zhang X, Liu M, Pielak GJ, Li C
Abstract
Protein mobility in living cells is vital for cell function. Both cytosolic viscosity and weak protein-protein interactions affect mobility, but examining viscosity and weak interaction effects is challenging....
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[NMR paper] Detection of a conformational change in maltose binding protein by (129)Xe NMR spectr
Detection of a conformational change in maltose binding protein by (129)Xe NMR spectroscopy.
Related Articles Detection of a conformational change in maltose binding protein by (129)Xe NMR spectroscopy.
J Am Chem Soc. 2001 Sep 5;123(35):8616-7
Authors: Rubin SM, Spence MM, Dimitrov IE, Ruiz EJ, Pines A, Wemmer DE
Intracellular environment can change protein conformational dynamics in cells through weak interactions - Science
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