[NMR paper] Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins
The comprehensive delineation of inherent dynamic motions embedded in proteins, which can be crucial for their functional repertoire, is often essential yet remains poorly understood in the majority of cases. In this protocol, we outline detailed descriptions of the necessary steps for employing solution NMR spectroscopy for the in-depth amino acid level understanding of backbone dynamics of proteins. We describe the application of the protocol on the structurally analogous Tudor domains with...
[NMR paper] A high-resolution description of ?1-adrenergic receptor functional dynamics and allosteric coupling from backbone NMR.
A high-resolution description of ?1-adrenergic receptor functional dynamics and allosteric coupling from backbone NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif Related Articles A high-resolution description of ?1-adrenergic receptor functional dynamics and allosteric coupling from backbone NMR.
Nat Commun. 2020 May 05;11(1):2216
Authors: Grahl A, Abiko LA, Isogai S, Sharpe T, Grzesiek S
Abstract
Signal transmission and regulation of G-protein-coupled receptors...
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05-07-2020 09:07 PM
[NMR paper] An NMR strategy to detect conformational differences in a protein complexed with highly analogous inhibitors in solution.
An NMR strategy to detect conformational differences in a protein complexed with highly analogous inhibitors in solution.
Related Articles An NMR strategy to detect conformational differences in a protein complexed with highly analogous inhibitors in solution.
Methods. 2018 Apr 12;:
Authors: Persons JD, Khan SN, Ishima R
Abstract
This manuscript presents an NMR strategy to investigate conformational differences in protein-inhibitor complexes, when the inhibitors tightly bind to a protein at sub-nanomolar dissociation constants...
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04-16-2018 11:40 PM
Solvent saturation transfer to proteins (SSTP) for structural and functional characterization of proteins
Solvent saturation transfer to proteins (SSTP) for structural and functional characterization of proteins
Abstract
Protein structure determination using NMR is dependent on experimentally acquired distance restraints. Often, however, an insufficient number of these restraints are available for determining a proteinâ??s correct fold, much less its detailed three-dimensional structure. In consideration of this problem, we propose a simple means to acquire supplemental structural restraints from protein surface accessibilities using solvent saturation...
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11-30-2017 05:01 PM
[NMR paper] Co-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR.
Co-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR.
Related Articles Co-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR.
Protein Expr Purif. 2017 Jul 24;:
Authors: Woestenenk E, Agback P, Unnerståle S, Henderson I, Agback T
Abstract
A novel approach for separate expression of dengue virus NS3 protease and its NS2B cofactor domain is described in this paper. The...
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07-29-2017 10:35 AM
[NMR paper] Solution NMR characterization of chemokine CXCL8/IL-8 monomer and dimer binding to glycosaminoglycans: structural plasticity mediates differential binding interactions.
Solution NMR characterization of chemokine CXCL8/IL-8 monomer and dimer binding to glycosaminoglycans: structural plasticity mediates differential binding interactions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-highwire.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution NMR characterization of chemokine CXCL8/IL-8 monomer and dimer binding to glycosaminoglycans: structural plasticity mediates...
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04-02-2016 09:55 PM
Exploring the Backbone Dynamics of Native Spider Silk Proteins in Black Widow Silk Glands with Solution-state NMR Spectroscopy
Exploring the Backbone Dynamics of Native Spider Silk Proteins in Black Widow Silk Glands with Solution-state NMR Spectroscopy
Publication date: Available online 13 June 2014
Source:Polymer</br>
Author(s): Dian Xu , Jeffery L. Yarger , Gregory P. Holland</br>
Spider dragline silk is an outstanding biopolymer with a strength that exceeds steel by weight and a toughness greater than high-performance fibers like Kevlar. For this reason, understanding how a spider converts the gel-like, aqueous protein spinning dope within the major ampullate (MA) gland into a super...
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06-14-2014 12:53 AM
Functional dynamics of proteins revealed by solution NMR
Functional dynamics of proteins revealed by solution NMR
October 2012
Publication year: 2012
Source:Current Opinion in Structural Biology, Volume 22, Issue 5</br>
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Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation...
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02-03-2013 10:13 AM
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
FEBS J. 2010 Sep 3;
Authors: Farina B, Pirone L, Russo L, Viparelli F, Doti N, Pedone C, Pedone EM, Fattorusso R
PED/PEA-15 (phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes) is a ubiquitously expressed protein and a key regulator of cell growth and glucose metabolism. PED/PEA-15 mediates both homotypic and heterotypic interactions and is constituted by...