Related ArticlesNMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes.
Extremophiles. 2001 Oct;5(5):303-11
Authors: Lamosa P, Brennan L, Vis H, Turner DL, Santos H
Rubredoxins are small, soluble proteins that display a wide variation in thermostability, despite having a high degree of sequence similarity They also vary in the extent to which they are stabilized by solutes such as diglycerol phosphate. Hence, they provide excellent models for studying the mechanisms of thermostabilization. Nuclear magnetic resonance (NMR) spectroscopy can be used to investigate interactions between molecules, as well as subtle changes in conformation in solution, and also provides a means to measure protein stability. The assignment of the proton NMR spectrum of the zinc rubredoxin from Desulfovibrio gigas is presented, together with its structure in solution. The stabilizing effect of diglycerol phosphate on rubredoxin is demonstrated and assessed by determining selected amide proton exchange rates; diglycerol phosphate at 100 mM concentration caused an additional structural stabilization of 1.2 +/-0.4 kJ/mol. The pattern of effects on the exchange rates is discussed in relation to the protein structure.
Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1148-53
Authors: Buchko GW, Hewitt SN, Napuli AJ, Van Voorhis WC, Myler PJ
Abstract
Owing to the evolution of multi-drug-resistant and extremely drug-resistant Mycobacterium tuberculosis strains,...
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[NMR paper] Structure of the model peptides of Bombyx mori silk-elastin like protein studied with
Structure of the model peptides of Bombyx mori silk-elastin like protein studied with solid state NMR.
Related Articles Structure of the model peptides of Bombyx mori silk-elastin like protein studied with solid state NMR.
Biomacromolecules. 2004 May-Jun;5(3):744-50
Authors: Ohgo K, Kurano TL, Kumashiro KK, Asakura T
The peptides (AG)(6)(VPGVG)(AG)(7) and (AG)(5)(VPGVG)(2)(AG)(5) are models for a new type of protein with both composition and properties such as Bombyx mori silk and elastin. In this paper, we report the solid-state NMR results...
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[NMR paper] Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by
Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by NMR spectroscopy and solution X-ray scattering and interactions with rubredoxin reductase.
Related Articles Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by NMR spectroscopy and solution X-ray scattering and interactions with rubredoxin reductase.
Biochemistry. 2004 Mar 23;43(11):3167-82
Authors: Perry A, Tambyrajah W, Grossmann JG, Lian LY, Scrutton NS
Here we provide insights into the molecular structure of the two-iron...
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[NMR paper] Crystal structure of the SH2 domain from the adaptor protein SHC: a model for peptide
Crystal structure of the SH2 domain from the adaptor protein SHC: a model for peptide binding based on X-ray and NMR data.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Crystal structure of the SH2 domain from the adaptor protein SHC: a model for peptide binding based on X-ray and NMR data.
J Mol Biol. 1995 Nov 17;254(1):86-95
Authors: Mikol V, Baumann G, Zurini MG, Hommel U
Src homology 2 domains (SH2) are protein molecules found within a wide variety of cytoplasmic...
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[NMR paper] Structure and dynamics of ferrocytochrome c553 from Desulfovibrio vulgaris studied by
Structure and dynamics of ferrocytochrome c553 from Desulfovibrio vulgaris studied by NMR spectroscopy and restrained molecular dynamics.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure and dynamics of ferrocytochrome c553 from Desulfovibrio vulgaris studied by NMR spectroscopy and restrained molecular dynamics.
J Mol Biol. 1995 Feb 3;245(5):661-81
Authors: Blackledge MJ, Medvedeva S, Poncin M, Guerlesquin F, Bruschi M, Marion D
The solution structure of...
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[NMR paper] A method for studying the structure of uniaxially aligned biopolymers using solid sta
A method for studying the structure of uniaxially aligned biopolymers using solid state 15N-nmr: application to Bombyx mori silk fibroin fibers.
Related Articles A method for studying the structure of uniaxially aligned biopolymers using solid state 15N-nmr: application to Bombyx mori silk fibroin fibers.
Biopolymers. 1993 May;33(5):847-61
Authors: Nicholson LK, Asakura T, Demura M, Cross TA
Recent advances in the application of solid state nmr spectroscopy to uniformly aligned biopolymers have opened a window through which to view the...
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[NMR paper] Comparison of the X-ray structure of native rubredoxin from Pyrococcus furiosus with
Comparison of the X-ray structure of native rubredoxin from Pyrococcus furiosus with the NMR structure of the zinc-substituted protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Comparison of the X-ray structure of native rubredoxin from Pyrococcus furiosus with the NMR structure of the zinc-substituted protein.
Protein Sci. 1992...
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[NMR paper] Solid-state NMR approaches for studying membrane protein structure.
Solid-state NMR approaches for studying membrane protein structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--arjournals.annualreviews.org-images-AnnualReviews100x25.gif Related Articles Solid-state NMR approaches for studying membrane protein structure.
Annu Rev Biophys Biomol Struct. 1992;21:25-47
Authors: Smith SO, Peersen OB
NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabili
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