[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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[NMR paper] "Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.
"Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.
Related Articles "Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.
Chemistry. 2015 Feb 12;
Authors: Fizil Á, Gáspári Z, Barna T, Marx F, Batta G
Abstract
Transition between conformational states in proteins is being recognized as a possible key factor...
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02-14-2015 03:52 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...
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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...
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11-08-2013 01:42 PM
[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...
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11-24-2010 09:01 PM
[NMR paper] Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide
Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide spin label and two-dimensional NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide spin label and two-dimensional NMR study.
J Biol Chem. 1999 Mar 26;274(13):8411-20
Authors: Yuan T, Ouyang H, Vogel HJ
Binding of calcium to calmodulin (CaM) causes a conformational...
Visualizing Side Chains of Invisible Protein Conformers by Solution NMR - ScienceDirect.com
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