[NMR paper] Methodological advancements for characterising protein side chains by NMR spectroscopy
Methodological advancements for characterising protein side chains by NMR spectroscopy
The surface of proteins is covered by side chains of polar amino acids that are imperative for modulating protein functionality through the formation of noncovalent intermolecular interactions. However, despite their tremendous importance, the unique structures of protein side chains require tailored approaches for investigation by nuclear magnetic resonance spectroscopy and so have traditionally been understudied compared with the protein backbone. Here, we review substantial recent...
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05-16-2021 02:19 AM
[NMR paper] Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy.
Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy.
Related Articles Characterising 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...
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04-17-2019 01:41 PM
[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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08-26-2017 03:38 PM
[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,...
Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy - Nature.com
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