Post-Translational Modifications of Protein Backbones:Unique Functions, Mechanisms, and Challenges
Post-Translational Modifications of Protein Backbones:Unique Functions, Mechanisms, and Challenges
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00861/20171103/images/medium/bi-2017-00861b_0001.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00861
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nmrlearner
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11-04-2017 12:23 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...
nmrlearner
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11-12-2013 03:52 PM
Visualizing Side-chains of Invisible Protein Conformers by Solution NMR
Visualizing Side-chains of Invisible Protein Conformers by Solution NMR
Publication date: Available online 8 November 2013
Source:Journal of Molecular Biology</br>
Author(s): Guillaume Bouvignies , Pramodh Vallurupalli , Lewis E. Kay</br>
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 standard biophysical...
Cell signaling, post-translational protein modifications and NMR spectroscopy
Cell signaling, post-translational protein modifications and NMR spectroscopy
Abstract Post-translationally modified proteins make up the majority of the proteome and establish, to a large part, the impressive level of functional diversity in higher, multi-cellular organisms. Most eukaryotic post-translational protein modifications (PTMs) denote reversible, covalent additions of small chemical entities such as phosphate-, acyl-, alkyl- and glycosyl-groups onto selected subsets of modifiable amino acids. In turn, these modifications induce highly specific changes in the chemical ...
nmrlearner
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09-29-2012 11:56 AM
Interactions of protein side chains with RNA defined with REDOR solid state NMR
Interactions of protein side chains with RNA defined with REDOR solid state NMR
Abstract Formation of the complex between human immunodeficiency virus type-1 Tat protein and the transactivation response region (TAR) RNA is vital for transcriptional elongation, yet the structure of the Tat-TAR complex remains to be established. The NMR structures of free TAR, and TAR bound to Tat-derived peptides have been obtained by solution NMR, but only a small number of intermolecular NOEs could be identified unambiguously, preventing the determination of a complete structure. Here we show that a...
nmrlearner
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09-27-2011 07:04 AM
[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...
nmrlearner
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11-24-2010 09:01 PM
[NMR paper] NMR analysis of the interaction between protein L and Ig light chains.
NMR analysis of the interaction between protein L and Ig light chains.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR analysis of the interaction between protein L and Ig light chains.
J Mol Biol. 1997 Jul 4;270(1):8-13
Authors: Enokizono J, Wikström M, Sjöbring U, Björck L, Forsén S, Arata Y, Kato K, Shimada I
Protein L is a cell wall protein expressed by some strains of the anaerobic bacterial species Peptostreptococcus magnus. It binds to immunoglobulin...
Light-driven post-translational installation of reactive protein side chains - Nature.com
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