Related ArticlesStructural investigation of pig metmyoglobin by 129Xe NMR spectroscopy.
Biochim Biophys Acta. 2004 Sep 24;1674(2):182-92
Authors: Corda M, Era B, Fais A, Casu M
The potentiality of xenon's sensitivity to its local magnetic environment is thoroughly investigated to probe internal structural differences between pig and horse metmyoglobin (MMb). These MMb's differ by 14 amino acids. One of these, Ile142 in horse MMb, is located in the proximal cavity, which is the xenon-binding site in horse MMb, and is replaced by Met142 in pig MMb. Specific and non-specific xenon-protein interactions are investigated here by 129Xe NMR chemical shifts and relaxation rate in aqueous solutions of pig MMb as a function of the xenon and protein concentrations. The results are complemented with 129Xe NMR data of the isostructural carbonmonoxy myoglobin (COMb), with computational calculations in order to highlight the structural differences between the cavities, and 1H NMR spectra to test the dependence of the 1H chemical shift on the addition of xenon. The 129Xe chemical shift NMR parameters are analysed quantitatively in terms of a two-site model. Xenon forms a 1:1 complex with the protein, characterized by an equilibrium binding constant K=[Xe]in/([Xe]out[MMb]), and exchanges rapidly between a cavity within the protein (X(ein)) and all other environments (Xe(out)). A comparison of equilibrium constant, K (74 M(-1)) in pig and K (146 M(-1)) in horse, reveals differences in affinity of xenon to the interior of pig MMb. Changes in xenon binding in both pig and horse MMb are also pointed out by other experimental results, e.g. the difference in the estimated delta(in), which is shifted downfield in pig MMb and upfield in horse MMb, with respect to 129Xe in buffer solution; the xenon-iron distance, 7.4 A, which is longer in the pig than was found in the horse, 5.3 A.
High-Pressure in Situ 129Xe NMR Spectroscopy and Computer Simulations of Breathing Transitions in the Metal–Organic Framework Ni2(2,6-ndc)2(dabco) (DUT-8(Ni))
High-Pressure in Situ 129Xe NMR Spectroscopy and Computer Simulations of Breathing Transitions in the Metal–Organic Framework Ni2(2,6-ndc)2(dabco) (DUT-8(Ni))
Herbert C. Hoffmann, Bassem Assfour, Fanny Epperlein, Nicole Klein, Silvia Paasch, Irena Senkovska, Stefan Kaskel, Gotthard Seifert and Eike Brunner
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201951t/aop/images/medium/ja-2011-01951t_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201951t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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[NMR paper] Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic eve
Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.
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J Am Chem Soc. 2005 Jun 8;127(22):8014-5
Authors: Schanda P, Brutscher B
We demonstrate for different protein samples that 2D 1H-15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle...
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[NMR paper] Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe
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Protein Sci. 2005 Apr;14(4):848-55
Authors: Lowery TJ, Doucleff M, Ruiz EJ, Rubin SM, Pines A, Wemmer DE
The chemical shift of the (129)Xe NMR signal has been shown to be extremely sensitive to the local environment around the atom and has been used to follow processes such as ligand binding by bacterial periplasmic binding proteins. Here we show...
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[NMR paper] First structural investigation of the restriction ribonuclease RegB: NMR spectroscopi
First structural investigation of the restriction ribonuclease RegB: NMR spectroscopic conditions, 13C/15N double-isotopic labelling and two-dimensional heteronuclear spectra.
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Protein Expr Purif. 2004 Mar;34(1):158-65
Authors: Saďda F, Odaert B, Uzan M, Bontems F
The bacteriophage T4 genome-encoded ribonuclease RegB is the unique well-defined restriction...
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[NMR paper] Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectr
Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy.
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J Mol Biol. 2002 Sep 13;322(2):425-40
Authors: Rubin SM, Lee SY, Ruiz EJ, Pines A, Wemmer DE
Xenon-binding sites in proteins have led to a number of applications of xenon in biochemical and structural studies. Here we further develop the utility of 129Xe NMR in characterizing specific xenon-protein interactions. The sensitivity of the 129Xe...
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Structural, NMR spectroscopic, and computational investigation of hemin loading in th
Structural, NMR spectroscopic, and computational investigation of hemin loading in the hemophore HasAp from Pseudomonas aeruginosa.
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J Am Chem Soc. 2010 Jul 21;132(28):9857-72
Authors: Jepkorir G, Rodríguez JC, Rui H, Im W, Lovell S, Battaile KP, Alontaga AY, Yukl ET, Moënne-Loccoz P, Rivera M
When challenged by low-iron conditions several Gram-negative pathogens secrete a hemophore (HasA) to scavenge...
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Towards a structural understanding of the smallest known oncoprotein: Investigation o
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Biochim Biophys Acta. 2010 Nov 9;
Authors: King G, Oates J, Patel D, van den Berg HA, Dixon AM
The homo-dimeric E5 protein from Bovine Papillomavirus activates the platelet-derived growth factor ? receptor through transmembrane (TM)...
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Solution structural investigation and conformation-activity relationship of BAM8-22 b
Solution structural investigation and conformation-activity relationship of BAM8-22 by NMR and molecular dynamics simulations.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution structural investigation and conformation-activity relationship of BAM8-22 by NMR and molecular dynamics simulations.
Bioorg Med Chem Lett. 2010 Feb 1;20(3):1260-2
Authors: Lv G, Dong S
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Structural investigation of pig metmyoglobin by 129Xe NMR spectroscopy.
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