Solution structure of the conserved hypothetical protein Rv2302 from Mycobacterium tuberculosis.

scientific article

Solution structure of the conserved hypothetical protein Rv2302 from Mycobacterium tuberculosis. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1128/JB.00460-06
P932PMC publication ID1540057
P698PubMed publication ID16885468
P5875ResearchGate publication ID6902274

P50authorChang-Yub KimQ46865887
Garry W BuchkoQ56808207
Thomas C. TerwilligerQ37391688
P2093author name stringMichael A Kennedy
P2860cites workConformation of twisted β-pleated sheets in proteinsQ47975901
Spectroscopic studies of zinc(II)- and cobalt(II)-associated Escherichia coli formamidopyrimidine-DNA glycosylase: extended X-ray absorption fine structure evidence for a metal-binding domain.Q50509102
A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments.Q52399778
Overexpression of heat-shock proteins reduces survival of Mycobacterium tuberculosis in the chronic phase of infectionQ58231674
Circular dichroism studies of distorted alpha-helices, twisted beta-sheets, and beta turnsQ68045178
Clustering of large hydrophobes in the hydrophobic core of two-stranded alpha-helical coiled-coils controls protein folding and stabilityQ73616170
THE ULTRAVIOLET CIRCULAR DICHROISM OF POLYPEPTIDESQ77059124
Drug resistant tuberculosisQ78322624
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequenceQ22122411
CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceQ24286950
Crystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationQ26778405
Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNAQ27638483
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxationQ27860508
Touring protein fold space with Dali/FSSPQ27860559
The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift dataQ27860592
1H, 13C and 15N chemical shift referencing in biomolecular NMRQ27860609
AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMRQ27860778
MOLMOL: a program for display and analysis of macromolecular structuresQ27860873
Protein backbone angle restraints from searching a database for chemical shift and sequence homologyQ27861108
Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarraysQ28487046
Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profilingQ28487482
ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic informationQ29547192
Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniquesQ29614703
Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzymeQ29616524
Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labelingQ29618924
Inference of protein function from protein structure.Q30349960
Influence of non-bonded parameters on the quality of NMR structures: a new force field for NMR structure calculationQ30603962
Protein dynamics from NMR.Q34019517
The TB structural genomics consortium: a resource for Mycobacterium tuberculosis biology.Q35195303
Reverse turns in peptides and proteins.Q40294614
A software tool for the prediction of Xaa-Pro peptide bond conformations in proteins based on 13C chemical shift statisticsQ44258185
Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): a dynamic description of the DNA/protein interface.Q45231846
P433issue16
P407language of work or nameEnglishQ1860
P921main subjectMycobacterium tuberculosisQ130971
P304page(s)5993-6001
P577publication date2006-08-01
P1433published inJournal of BacteriologyQ478419
P1476titleSolution structure of the conserved hypothetical protein Rv2302 from Mycobacterium tuberculosis.
P478volume188

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cites work (P2860)
Q36946982Botulinum Neurotoxin Serotype A Recognizes Its Protein Receptor SV2 by a Different Mechanism than Botulinum Neurotoxin B Synaptotagmin
Q36030062Chemical shift assignments for Rv0577, a putative glyoxylase associated with virulence from Mycobacterium tuberculosis
Q27666231Inaugural structure from the DUF3349 superfamily of proteins, Mycobacterium tuberculosis Rv0543c
Q38600139Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.
Q86842994Solution structure of Rv0569, potent hypoxic signal transduction protein, from Mycobacterium tuberculosis
Q27661119Solution structure of Rv2377c-founding member of the MbtH-like protein family

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