[NMR paper] Backbone NMR assignments of tryparedoxin, the central protein in the hydroperoxide detoxification cascade of African trypanosomes, in the oxidized and reduced form.
Backbone NMR assignments of tryparedoxin, the central protein in the hydroperoxide detoxification cascade of African trypanosomes, in the oxidized and reduced form.
Related Articles Backbone NMR assignments of tryparedoxin, the central protein in the hydroperoxide detoxification cascade of African trypanosomes, in the oxidized and reduced form.
Biomol NMR Assign. 2017 Jun 01;:
Authors: Wagner A, Diehl E, Krauth-Siegel RL, Hellmich UA
Abstract
Tryparedoxin (Tpx) is a pivotal protein in the redox-metabolism of trypanosomatid...
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Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress - Phys.Org
Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress - Phys.Org
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Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress
Phys.Org
Structural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain. Credit: Wiley. A special type of small sulfur-rich protein, metallothioneins, have an extraordinary capability for ...
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[NMR paper] Sequential protein NMR assignments in the liquid state via sequential data acquisition.
Sequential protein NMR assignments in the liquid state via sequential data acquisition.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Sequential protein NMR assignments in the liquid state via sequential data acquisition.
J Magn Reson. 2013 Dec 14;239C:23-28
Authors: Wiedemann C, Bellstedt P, Kirschstein A, Häfner S, Herbst C, Görlach M, Ramachandran R
Abstract
Two different NMR pulse schemes involving sequential (1)H data acquisition are...
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[NMR paper] Sequential protein NMR assignments in the liquid state via sequential data acquisition
Sequential protein NMR assignments in the liquid state via sequential data acquisition
Publication date: Available online 14 December 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Christoph Wiedemann , Peter Bellstedt , Anika Kirschstein , Sabine Häfner , Christian Herbst , Matthias Görlach , Ramadurai Ramachandran</br>
Two different NMR pulse schemes involving sequential 1H data acquisition are presented for achieving protein backbone sequential resonance assignments: (i) acquisition of 3D {HCCNH & HNCACONH} and (ii) collection of 3D {HNCOCANH &...
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[NMR paper] Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
Related Articles Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
J Biomol NMR. 2013 Apr 23;
Authors: Chakravorty DK, Wang B, Lee CW, Guerra AJ, Giedroc DP, Merz KM
Abstract
Correctly calculating the structure of metal coordination sites in a protein during the process of nuclear magnetic resonance (NMR) structure determination and refinement continues to...
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Simultaneous acquisition of 13Cαâ??15N and 1Hâ??15Nâ??15N sequential correlations in proteins: application of dual receivers in 3D HNN
Simultaneous acquisition of 13Cαâ??15N and 1Hâ??15Nâ??15N sequential correlations in proteins: application of dual receivers in 3D HNN
Abstract We describe here, adaptation of the HNN pulse sequence for multiple nuclei detection using two independent receivers by utilizing the detectable 13Cα transverse magnetization which was otherwise dephased out in the conventional HNN experiment. It enables acquisition of 2D 13Cαâ??15N sequential correlations along with the standard 3D 15Nâ??15Nâ??1H correlations, which provides directionality to sequential walk in HNN, on one hand, and enhances...
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[NMR paper] Folding Trp-cage to NMR resolution native structure using a coarse-grained protein mo
Folding Trp-cage to NMR resolution native structure using a coarse-grained protein model.
Related Articles Folding Trp-cage to NMR resolution native structure using a coarse-grained protein model.
Biophys J. 2005 Jan;88(1):147-55
Authors: Ding F, Buldyrev SV, Dokholyan NV
We develop a coarse-grained protein model with a simplified amino acid interaction potential. Using this model, we perform discrete molecular dynamics folding simulations of a small 20-residue protein--Trp-cage--from a fully extended conformation. We demonstrate the ability...
A Dual-Metal-Catalyzed Sequential Cascade Reaction in an Engineered Protein Cage
Linear Mode
