[NMR paper] NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics.
NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png 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 NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests...
nmrlearner
Journal club
0
05-24-2016 11:36 AM
Exploring Folding Cooperativity of a Repeat Protein Folding by 2D-NMR Detected Pressure Perturbation
Exploring Folding Cooperativity of a Repeat Protein Folding by 2D-NMR Detected Pressure Perturbation
Publication date: 16 February 2016
Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br>
Author(s): Martin J. Fossat, Angel Garcia, Doug Barrick, Christian Roumestand, Catherine A. Royer</br>
</br></br>
</br></br>
More...
[NMR paper] Automated resonance assignment of the 21kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA
Automated resonance assignment of the 21kDa stereo-array isotope labeled thioldisulfide oxidoreductase DsbA
Publication date: December 2014
Source:Journal of Magnetic Resonance, Volume 249</br>
Author(s): Elena Schmidt , Teppei Ikeya , Mitsuhiro Takeda , Frank Löhr , Lena Buchner , Yutaka Ito , Masatsune Kainosho , Peter Güntert</br>
The automated chemical shift assignment algorithm FLYA has been extended for use with stereo-array isotope labeled (SAIL) proteins to determine the sequence-specific resonance assignments of large proteins. Here we present the...
nmrlearner
Journal club
0
11-14-2014 08:33 AM
[NMR paper] Solid-State NMR Study of a 41 kDa Membrane Protein Complex DsbA/DsbB.
Solid-State NMR Study of a 41 kDa Membrane Protein Complex DsbA/DsbB.
Related Articles Solid-State NMR Study of a 41 kDa Membrane Protein Complex DsbA/DsbB.
J Phys Chem B. 2013 Mar 25;
Authors: Sperling LJ, Tang M, Berthold DA, Nesbitt AE, Gennis RB, Rienstra CM
Abstract
The disulfide bond generation system in E. coli is led by a periplasmic protein DsbA and an integral membrane protein DsbB. Here we present a solid-state NMR (SSNMR) study of a 41 kDa membrane protein complex DsbA/DsbB precipitated in the presence of native lipids to...
nmrlearner
Journal club
0
03-27-2013 03:33 PM
NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554.
NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554.
NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554.
Protein Sci. 2011 Apr 21;
Authors: Atia-Tul-Wahab , Serrano P, Geralt M, Wüthrich K
The solution structure of the hypothetical phage-related protein NP_888769.1 from the gram-negative bacterium Bordetella bronchoseptica contains a well-structured core comprising a five-stranded, antiparallel ?-sheet packed...
nmrlearner
Journal club
0
04-27-2011 04:03 PM
[NMR paper] Redesign of a four-helix bundle protein by phage display coupled with proteolysis and
Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography.
Related Articles Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and X-ray crystallography.
J Mol Biol. 2002 Oct 18;323(2):253-62
Authors: Chu R, Takei J, Knowlton JR, Andrykovitch M, Pei W, Kajava AV, Steinbach PJ, Ji X, Bai Y
To test whether it is practical to use phage display coupled with proteolysis for protein design, we...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] Characterization of polyacrylamide-stabilized Pfl phage liquid crystals for protein N
Characterization of polyacrylamide-stabilized Pfl phage liquid crystals for protein NMR spectroscopy.
Related Articles Characterization of polyacrylamide-stabilized Pfl phage liquid crystals for protein NMR spectroscopy.
J Biomol NMR. 2002 Jan;22(1):83-7
Authors: Trempe JF, Morin FG, Xia Z, Marchessault RH, Gehring K
A new polymer-stabilized nematic liquid crystal has been characterized for the measurement of biomolecular residual dipolar couplings. Filamentous Pf1 phage were embedded in a polyacrylamide matrix that fixes the orientation of...