When Heterotrimeric G Proteins Are Not Activated by G Protein-Coupled Receptors: Structural Insights and Evolutionary Conservation
When Heterotrimeric G Proteins Are Not Activated by G Protein-Coupled Receptors: Structural Insights and Evolutionary Conservation
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Biochemistry
DOI: 10.1021/acs.biochem.7b00845
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nmrlearner
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10-17-2017 10:19 AM
Variability and conservation of structural domains in divide-and-conquer approaches
Variability and conservation of structural domains in divide-and-conquer approaches
Abstract
The use of protein building blocks for the structure determination of multidomain proteins and proteinâ??protein complexes, also known as the â??divide and conquerâ?? approach, is an important strategy for obtaining protein structures. Atomic-resolution X-ray or NMR data of the individual domains are combined with lower-resolution electron microscopy maps or X-ray data of the full-length protein or the protein complex. Doing so, it is often assumed that the...
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05-30-2016 01:15 PM
[NMR paper] A ¹H NMR study of the specificity of ?-l-arabinofuranosidases on natural and unnatural substrates.
A ¹H NMR study of the specificity of ?-l-arabinofuranosidases on natural and unnatural substrates.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A ¹H NMR study of the specificity of ?-l-arabinofuranosidases on natural and unnatural substrates.
Biochim Biophys Acta. 2014 Oct;1840(10):3106-14
Authors: Borsenberger V, Dornez E, Desrousseaux ML, Massou S, Tenkanen M, Courtin CM, Dumon C, O'Donohue MJ, Fauré R
Abstract
BACKGROUND: The...
nmrlearner
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10-18-2014 09:26 PM
[NMR paper] Amino acid conservation and interactions in rhodopsin: Probing receptor activation by NMR spectroscopy.
Amino acid conservation and interactions in rhodopsin: Probing receptor activation by NMR spectroscopy.
Related Articles Amino acid conservation and interactions in rhodopsin: Probing receptor activation by NMR spectroscopy.
Biochim Biophys Acta. 2013 Oct 29;
Authors: Pope A, Eilers M, Reeves PJ, Smith SO
Abstract
Rhodopsin is a classical two-state G protein-coupled receptor (GPCR). In the dark, its 11-cis retinal chromophore serves as an inverse agonist to lock the receptor in an inactive state. Retinal-protein and protein-protein...
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11-05-2013 06:53 PM
[NMR images] Biodiversity : Use and Conservation : Nuclear Magnetic Resonance: An ...
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Biodiversity : Use and Conservation : Nuclear Magnetic Resonance: An ...
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[NMR paper] Correlation between 2H NMR side-chain order parameters and sequence conservation in g
Correlation between 2H NMR side-chain order parameters and sequence conservation in globular proteins.
Related Articles Correlation between 2H NMR side-chain order parameters and sequence conservation in globular proteins.
J Am Chem Soc. 2003 Jul 30;125(30):9004-5
Authors: Mittermaier A, Davidson AR, Kay LE
Side-chain 2H NMR relaxation data have been collected for the SH3 domain from the Fyn tyrosine kinase and analyzed with respect to sequence preference and per-residue solvent accessibility. Residues that are highly preferred at a given...
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11-24-2010 09:16 PM
[MWClarkson blog] Dynamics conservation in the Ras superfamily
Dynamics conservation in the Ras superfamily
http://www.researchblogging.org/public/citation_icons/rb2_large_gray.pngThe proposition that general fold architecture is preserved within a family of evolutionarily-related proteins is not controversial. The amino acid sequence of a protein determines its structure, and countless studies have substantiated the idea that proteins with similar sequences will adopt similar folded conformations. Because structure and dynamics are intrinsically linked, one could reasonably assume that many features of a protein's dynamics get conserved along with...
Conservation of Specificity in Two Low-SpecificityProteins
Linear Mode
