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...
[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...
[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,...
nmrlearner
Journal club
0
01-29-2014 02:01 PM
[NMR paper] Visualizing Side-chains of Invisible Protein Conformers by Solution NMR.
Visualizing Side-chains of Invisible Protein Conformers by Solution NMR.
Related Articles Visualizing Side-chains of Invisible Protein Conformers by Solution NMR.
J Mol Biol. 2013 Nov 7;
Authors: Bouvignies G, Vallurupalli P, Kay LE
Abstract
Sparsely populated and transiently formed protein conformers can play key roles in many biochemical processes. Understanding the structure function paradigm requires, therefore, an atomic resolution description of these rare states. Yet they are difficult to study because they cannot be observed using...
[NMR paper] The effects of mutations on motions of side-chains in protein L studied by 2H NMR dyn
The effects of mutations on motions of side-chains in protein L studied by 2H NMR dynamics and scalar couplings.
Related Articles The effects of mutations on motions of side-chains in protein L studied by 2H NMR dynamics and scalar couplings.
J Mol Biol. 2003 Jun 6;329(3):551-63
Authors: Millet O, Mittermaier A, Baker D, Kay LE
Recently developed 2H spin relaxation experiments are applied to study the dynamics of methyl-containing side-chains in the B1 domain of protein L and in a pair of point mutants of the domain, F22L and A20V. X-ray and...
Methodological advancements for characterising protein side chains by NMR spectroscopy
Linear Mode
