Related ArticlesWeak 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 crystallography or solution NMR. Solid-state NMR does not suffer from the molecular size limitations affecting solution NMR, and it can be applied to molecules in different aggregation states, including non-crystalline precipitates and sediments. A solid-state NMR approach based on high magnetic fields, fast magic-angle sample spinning, and deuteration provides chemical-shift and relaxation mapping that enabled the characterization of the structure and dynamics of the transient association between two regions in an 80 kDa protein assembly. This led to direct verification of a mechanism of regulation of E. coli DNA metabolism.
PMID: 27101578 [PubMed - as supplied by publisher]
[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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08-08-2013 03:46 PM
[NMR paper] NMR studies of weak protein-protein interactions.
NMR studies of weak protein-protein interactions.
NMR studies of weak protein-protein interactions.
Prog Nucl Magn Reson Spectrosc. 2013 May;71:59-72
Authors: Lian LY
PMID: 23611315
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NMR Studies of Weak Protein-Protein Interactions
NMR Studies of Weak Protein-Protein Interactions
Available online 20 December 2012
Publication year: 2012
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
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12-20-2012 04:48 PM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these interactions...
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09-30-2011 06:00 AM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these...
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09-30-2011 05:59 AM
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
Top Curr Chem. 2011 Aug 2;
Authors: Vinogradova O, Qin J
Protein-protein interactions are crucial for a wide variety of biological processes. These interactions range from high affinity (K (d) < nM) to very low affinity (K (d) > mM). While much is known about the nature of high affinity protein complexes, our knowledge about structural characteristics...
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08-03-2011 12:00 PM
[NMR paper] Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spec
Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.
Related Articles Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.
J Mol Biol. 2004 Aug 13;341(3):869-79
Authors: Thiriot DS, Nevzorov AA, Zagyanskiy L, Wu CH, Opella SJ
The atomic resolution structure of Pf1 coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles in solution is compared to the structures previously determined by X-ray fiber and...
Weak and Transient Protein Interactions Determined by Solid-State NMR.
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