Related ArticlesThe 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 Jun 30;1412(2):139-48
Authors: Quirk PG, Smith KJ, Thomas CM, Jackson JB
The dI component of transhydrogenase binds NAD+ and NADH. A mobile loop region of dI plays an important role in the nucleotide binding process, and mutations in this region result in impaired hydride transfer in the complete enzyme. We have previously employed one-dimensional 1H-NMR spectroscopy to study wild-type and mutant dI proteins of Rhodospirillum rubrum and the effects of nucleotide binding. Here, we utilise two- and three-dimensional NMR experiments to assign the signals from virtually all of the backbone and side-chain protons of the loop residues. The mobile loop region encompasses 17 residues: Asp223-Met239. The assignments also provide a much strengthened basis for interpreting the structural changes occurring upon nucleotide binding, when the loop closes down onto the surface of the protein and loses mobility. The role of the mobile loop region in catalysis is discussed with particular reference to a newly-developed model of the dI protein, based on its homology with alanine dehydrogenase.
[NMR paper] Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cel
Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cells are modulated by rafts.
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Cancer Cell Int. 2005 Feb 9;5(1):2
Authors: Mannechez A, Reungpatthanaphong P, de Certaines JD, Leray G, Le Moyec L
BACKGROUND: Most cancer cells are characterized by mobile lipids visible on proton NMR (1H-NMR), these being comprised mainly of methyl and methylene signals from lipid acyl chains....
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[NMR paper] Proton-translocating carboxyl of subunit c of F1Fo H(+)-ATP synthase: the unique envi
Proton-translocating carboxyl of subunit c of F1Fo H(+)-ATP synthase: the unique environment suggested by the pKa determined by 1H NMR.
Related Articles Proton-translocating carboxyl of subunit c of F1Fo H(+)-ATP synthase: the unique environment suggested by the pKa determined by 1H NMR.
Biochemistry. 1995 Dec 12;34(49):16186-93
Authors: Assadi-Porter FM, Fillingame RH
Subunit c of the H(+)-transporting F1Fo ATP synthase (EC 3.6.1.34) is thought to fold across the membrane as a hairpin of two alpha helices with a conserved Asp/Glu residue,...
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[NMR paper] Structural and dynamic characterization of the phosphotyrosine binding region of a Sr
Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain--phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches.
Related Articles Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain--phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches.
Biochemistry. 1995 Sep 12;34(36):11353-62
Authors: Pascal SM, Yamazaki T, Singer AU, Kay LE, Forman-Kay JD
Arginine side chains are often...
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[NMR paper] A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escheric
A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli.
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 A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli.
Protein Sci. 1993 Nov;2(11):1938-47
Authors: Sun ZY, Truong HT, Pratt EA, Sutherland DC,...
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[NMR paper] Proton-transfer effects in the active-site region of Escherichia coli thioredoxin usi
Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.
Related Articles Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.
Biochemistry. 1991 Apr 30;30(17):4262-8
Authors: Dyson HJ, Tennant LL, Holmgren A
A series of two-dimensional (2D) correlated 1H NMR spectra of reduced and oxidized Escherichia coli thioredoxin have been used to probe the effects of pH in the vicinity of the active site, -Cys32-Gly-Pro-Cys35-, using the...
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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] Structural changes in the recombinant, NADP(H)-binding component of proton translocat
Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural 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...
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[NMR paper] The structure of the site on adenovirus early region 1A responsible for binding to TA
The structure of the site on adenovirus early region 1A responsible for binding to TATA-binding protein determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles The structure of the site on adenovirus early region 1A responsible for binding to TATA-binding protein determined by NMR spectroscopy.
J Biol Chem. 1999 Feb 5;274(6):3503-12
Authors: Molloy DP, Smith KJ, Milner AE, Gallimore PH, Grand RJ
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