Related ArticlesStructural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy.
FEBS Lett. 1999 Mar 5;446(1):127-32
Authors: Quirk PG, Jeeves M, Cotton NP, Smith JK, Jackson BJ
We have analysed 1H, 15N-HSQC spectra of the recombinant, NADP(H)-binding component of transhydrogenase in the context of the emerging three dimensional structure of the protein. Chemical shift perturbations of amino acid residues following replacement of NADP+ with NADPH were observed in both the adenosine and nicotinamide parts of the dinucleotide binding site and in a region which straddles the protein. These observations reflect the structural changes resulting from hydride transfer. The interactions between the recombinant, NADP(H)-binding component and its partner, NAD(H)-binding protein, are complicated. Helix B of the recombinant, NADP(H)-binding component may play an important role in the binding process.
Visualizing the principal component of 1H,15N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C
Visualizing the principal component of 1H,15N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C
Abstract Laboratories often repeatedly determine the structure of a given protein under a variety of conditions, mutations, modifications, or in a number of states. This approach can be cumbersome and tedious. Given then a database of structures, identifiers, and corresponding 1H,15N-HSQC NMR spectra for homologous proteins, we investigated whether structural information could be ascertained for a new homolog solely from its...
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Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
J Biomol NMR. 2011 Sep;51(1-2):115-22
Authors: Robertson IM, Boyko RF, Sykes BD
Abstract
Laboratories often repeatedly determine the structure of a given protein under a variety of conditions,...
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Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
J Biomol NMR. 2011 Sep;51(1-2):115-22
Authors: Robertson IM, Boyko RF, Sykes BD
Abstract
Laboratories often repeatedly determine the structure of a given protein under a variety of conditions,...
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09-30-2011 05:59 AM
[NMR paper] Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking.
Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking.
Related Articles Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking.
FEBS Lett. 2005 Aug 29;579(21):4585-90
Authors: Palma PN, Lagoutte B, Krippahl L, Moura JJ, Guerlesquin F
Ferredoxin (Fd) and ferredoxin-NADP(+)-reductase (FNR) are two terminal physiological partners of the photosynthetic electron transport chain. Based on a nuclear magnetic resonance...
[NMR paper] Binding of sucrose octasulphate to the C-type lectin-like domain of the recombinant n
Binding of sucrose octasulphate to the C-type lectin-like domain of the recombinant natural killer cell receptor NKR-P1A observed by NMR spectroscopy.
Related Articles Binding of sucrose octasulphate to the C-type lectin-like domain of the recombinant natural killer cell receptor NKR-P1A observed by NMR spectroscopy.
Chembiochem. 2002 Nov 4;3(11):1072-7
Authors: Kogelberg H, Frenkiel TA, Birdsall B, Chai W, Muskett FW
NKR-P1A is a C-type lectin-like receptor on natural killer cells believed to be involved in the cytotoxicity of these cells....
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[NMR paper] RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprote
RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.
Proc Natl Acad Sci U S A. 1991 Mar 15;88(6):2495-9
Authors: Hoffman DW, Query CC, Golden BL, White...
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[NMR paper] The mobile loop region of the NAD(H) binding component (dI) of proton-translocating n
The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
Biochim Biophys Acta. 1999...
Structural changes in the recombinant, NADP(H)-binding component of proton translocat
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