Related ArticlesCharacterising side chains in large proteins by protonless 13C-detected NMR spectroscopy.
Nat Commun. 2019 Apr 15;10(1):1747
Authors: Pritchard RB, Hansen DF
Abstract
Side chains cover protein surfaces and are fundamental to processes as diverse as substrate recognition, protein folding and enzyme catalysis. However, characterisation of side-chain motions has so far been restricted to small proteins and methyl-bearing side chains. Here we present a class of methods, based on 13C-detected NMR spectroscopy, to more generally quantify motions and interactions of side chains in medium-to-large proteins. A single, uniformly isotopically labelled sample is sufficient to characterise the side chains of six different amino acid types. Side-chain conformational dynamics on the millisecond time-scale can be quantified by incorporating chemical exchange saturation transfer (CEST) into the presented methods, whilst long-range 13C-13C scalar couplings reporting on nanosecond to millisecond motions can be quantified in proteins as large as 80 kDa. The presented class of methods promises characterisation of side-chain behaviour at a level that has so far been reserved for the protein backbone.
[NMR paper] Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Related Articles Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Chem Commun (Camb). 2017 Aug 25;:
Authors: Gerecht K, Figueiredo AM, Hansen DF
Abstract
Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the N?-C? bond of...
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[NMR paper] Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit.
Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit.
Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit.
Chem Commun (Camb). 2016 Jul 7;
Authors: Kurauskas V, Crublet E, Macek P, Kerfah R, Gauto DF, Boisbouvier J, Schanda P
Abstract
Solid-state NMR spectroscopy allows the characterization of the structure, interactions and dynamics of insoluble...
[NMR paper] Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
Angew Chem Int Ed Engl. 2013 Mar 11;52(11):3145-7
Authors: Werbeck ND, Kirkpatrick J,...
On the calculation of 3Jαβ-coupling constants for side chains in proteins
On the calculation of 3Jαβ-coupling constants for side chains in proteins
Abstract Structural knowledge about proteins is mainly derived from values of observables, measurable in NMR spectroscopic or X-ray diffraction experiments, i.e. absorbed or scattered intensities, through theoretically derived relationships between structural quantities such as atom positions or torsional angles on the one hand and observable quantities such as squared structure factor amplitudes, NOE intensities or 3 J-coupling constants on the other. The standardly used relation connecting 3 J-couplings...
Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy.
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