Related ArticlesComplete 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
Authors: Sun C, Holmgren A, Bushweller JH
Human glutaredoxin is a member of the glutaredoxin family, which is characterized by a glutathione binding site and a redox-active dithiol/disulfide in the active site. Unlike Escherichia coli glutaredoxin-1, this protein has additional cysteine residues that have been suggested to play a regulatory role in its activity. Human glutaredoxin (106 amino acid residues, M(r) = 12,000) has been purified from a pET expression vector with both uniform 15N labeling and 13C/15N double labeling. The combination of three-dimensional 15N-edited TOCSY, 15N-edited NOESY, HNCA, HN(CO)CA, and gradient sensitivity-enhanced HNCACB and HNCO spectra were used to obtain sequential assignments for residues 2-106 of the protein. The gradient-enhanced version of the HCCH-TOCSY pulse sequence and HCCH-COSY were used to obtain side chain 1H and 13C assignments. The secondary structural elements in the reduced protein were identified based on NOE information, amide proton exchange data, and chemical shift index data. Human glutaredoxin contains five helices extending approximately from residues 4-10, 24-36, 53-64, 83-92, and 94-104. The secondary structure also shows four beta-strands comprised of residues 15-19, 43-48, 71-75, 78-80, which form a beta-sheet almost identical to that found in E. coli glutaredoxin-1. Complete 1H, 13C, and 15N assignments and the secondary structure of fully reduced human glutaredoxin are presented. Comparison to the structures of other glutaredoxins is presented and differences in the secondary structure elements are discussed.
[NMR paper] Sequence-specific 1H NMR resonance assignments and secondary structure of human apoli
Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate.
Related Articles Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate.
Biochem Cell Biol. 1998;76(2-3):267-75
Authors: Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ
Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein distributed mainly in high and very low density lipoprotein. In this report we...
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[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] 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, 13C, and 15N NMR resonance assignments, secondary structure, and backbone topolog
1H, 13C, and 15N NMR resonance assignments, secondary structure, and backbone topology of a variant of human interleukin-3.
Related Articles 1H, 13C, and 15N NMR resonance assignments, secondary structure, and backbone topology of a variant of human interleukin-3.
Biochemistry. 1995 May 16;34(19):6540-51
Authors: Feng Y, Klein BK, Vu L, Aykent S, McWherter CA
Interleukin-3 (IL-3) is a cytokine which stimulates the proliferation and differentiation of hematopoietic progenitors into multiple cell lineages. The 1H, 15N, and 13C NMR resonances of...
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[NMR paper] Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue s
Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus.
Related Articles Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus.
J Biomol NMR. 1995 Apr;5(3):259-70
Authors: Fogh RH, Schipper D, Boelens R, Kaptein R
The 1H, 13C and 15N NMR resonances of serine protease PB92 have been assigned using 3D triple-resonance NMR techniques. With a molecular weight of 27 kDa (269 residues) this...
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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] 1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon
1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma.
Related Articles 1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma.
Biochemistry. 1992 Sep 8;31(35):8180-90
Authors: Grzesiek S, Döbeli H, Gentz R, Garotta G, Labhardt AM, Bax A
1H, 13C, and 15N NMR assignments of the protein backbone of human interferon-gamma, a homodimer of 31.4 kDa, have been made using the recently introduced three-dimensional (3D) triple-resonance NMR techniques. It is shown that, despite...
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[NMR paper] Complete sequence-specific 1H NMR assignments for human insulin.
Complete sequence-specific 1H NMR assignments for human insulin.
Related Articles Complete sequence-specific 1H NMR assignments for human insulin.
Biochemistry. 1990 Mar 27;29(12):2906-13
Authors: Kline AD, Justice RM
Solvent conditions where human insulin could be studied by high-resolution NMR were determined. Both low pH and addition of acetonitrile were required to overcome the protein's self-association and to obtain useful spectra. Two hundred eighty-six 1H resonances were located and assigned to specific sites on the protein by using...
Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human
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