Related Articles1H and 15N resonance assignments and solution secondary structure of oxidized Desulfovibrio vulgaris flavodoxin determined by heteronuclear three-dimensional NMR spectroscopy.
J Biomol NMR. 1993 Mar;3(2):133-49
Authors: Stockman BJ, Euvrard A, Kloosterman DA, Scahill TA, Swenson RP
Sequence-specific 1H and 15N resonance assignments have been made for all 145 non-prolyl residues and for the flavin cofactor in oxidized Desulfovibrio vulgaris flavodoxin. Assignments were obtained by recording and analyzing 1H-15N heteronuclear three-dimensional NMR experiments on uniformly 15N-enriched protein, pH 6.5, at 300 K. Many of the side-chain resonances have also been assigned. Observed medium-and long-range NOEs, in combination with 3JNH alpha coupling constants and 1HN exchange data, indicate that the secondary structure consists of a five-stranded parallel beta-sheet and four alpha-helices, with a topology identical to that determined previously by X-ray crystallographic methods. One helix, which is distorted in the X-ray structure, is non-regular in solution as well. Several protein-flavin NOEs, which serve to dock the flavin ligand to its binding site, have also been identified. Based on fast-exchange into 2H2O, the 1HN3 proton of the isoalloxazine ring is solvent accessible and not strongly hydrogen-bonded in the flavin binding site, in contrast to what has been observed in several other flavodoxins. The resonance assignments presented here can form the basis for assigning single-site mutant flavodoxins and for correlating structural differences between wild-type and mutant flavodoxins with altered redox potentials.
[NMR paper] Multinuclear NMR resonance assignments and the secondary structure of Escherichia col
Multinuclear NMR resonance assignments and the secondary structure of Escherichia coli thioesterase/protease I: a member of a new subclass of lipolytic enzymes.
Related Articles Multinuclear NMR resonance assignments and the secondary structure of Escherichia coli thioesterase/protease I: a member of a new subclass of lipolytic enzymes.
J Biomol NMR. 1998 May;11(4):363-80
Authors: Lin TH, Chen C, Huang RF, Lee YL, Shaw JF, Huang TH
Escherichia coli thioesterase/protease I is a 183 amino acid protein with a molecular mass of 20,500. This...
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[NMR paper] NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavo
NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin.
Eur J Biochem. 1997 Mar 1;244(2):384-99
Authors: Ponstingl H, Otting G
Recombinant flavodoxin from Escherichia coli was uniformly enriched with 15N and 13C isotopes and its oxidized form in aqueous...
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[NMR paper] Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human
Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form.
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 Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form.
Protein Sci. 1997 Feb;6(2):383-90
...
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[NMR paper] NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavo
NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin.
Eur J Biochem. 1997 Mar 1;244(2):384-99
Authors: Ponstingl H, Otting G
Recombinant flavodoxin from Escherichia coli was uniformly enriched with 15N and 13C isotopes and its oxidized form in aqueous...
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08-22-2010 03:03 PM
[NMR paper] Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human
Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form.
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 Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form.
Protein Sci. 1997 Feb;6(2):383-90
...
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[NMR paper] 1H and 15N NMR resonance assignments and solution secondary structure of oxidized Des
1H and 15N NMR resonance assignments and solution secondary structure of oxidized Desulfovibrio desulfuricans flavodoxin.
Related Articles 1H and 15N NMR resonance assignments and solution secondary structure of oxidized Desulfovibrio desulfuricans flavodoxin.
J Biomol NMR. 1996 May;7(3):225-35
Authors: Pollock JR, Swenson RP, Stockman BJ
Sequence-specific 1H and 15N resonance assignments have been made for 137 of the 146 nonprolyl residues in oxidized Desulfovibrio desulfuricans flavodoxin. Assignments were obtained by a concerted analysis...
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[NMR paper] 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.
1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.
Related Articles 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.
Biochemistry. 1992 Sep 22;31(37):8906-15
Authors: Okon M, Bray P, VuceliÄ? D
Sequence-specific resonance assignments of human beta 2-microglobulin (M(r) 12,000) and its secondary structure are determined by 2D NMR techniques. The protein is found to contain two antiparallel beta-sheets each of four beta-strands with the beta-sheets being connected by a...
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[NMR paper] Sequence-specific 1H NMR assignments and secondary structure in solution of Escherich
Sequence-specific 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor.
Related Articles Sequence-specific 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor.
Biochemistry. 1990 Jul 10;29(27):6332-41
Authors: Arrowsmith CH, Pachter R, Altman RB, Iyer SB, Jardetzky O
Sequence-specific 1H NMR assignments are reported for the active L-tryptophan-bound form of Escherichia coli trp repressor. The repressor is a symmetric dimer of 107 residues per monomer; thus at 25 kDa, this...