Xem 1-12 trên 12 kết quả Model of nmr.
  • uclear magnetic resonance spectroscopy can now be used to investigate the biochemical energetics of human tissues and organs noninvasively. The method already has increased our understanding of some muscle diseases, has provided information from muscle metabolism about whole-body functions, control, and hormonal status, has helped in the elucidation of hitherto unrecognized causes of disease, and yielded new ideas about the control of bioenergetics in vivo. Studies on the biochemistry of human brain, liver, heart, and kidney are just beginning.

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  • In the Biomedical Applications of Biophysics, Volume 3 of the Handbook of Modern Biophysics, the authors have added to the topics introduced in Volume 1, Fundamental Concepts in Biophysics. These additional topics help trace the broad field of biophysics. Patrice Koehl starts the book with an introduction to protein structure prediction based on energetics, homology modeling, and ab-initio calculations. Dickey and Faller follow with a “how-to approach” to model biomembranes.

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  • Heteronuclear NMR relaxation measurements and hydro-gen exchange data have been used to characterize protein dynamics in the presence or absence of stabilizing solutes from hyperthermophiles. Rubredoxin from Desulfovibrio gigaswas selected as a model protein and the effect of diglycerol phosphate on its dynamic behaviour was studied. The presence of 100 mMdiglycerol phosphate induces a fourfold increase in the half-life for thermal denaturation ofD.

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  • With the amount of genetic information available, a lot of attention has focused on systems biology, in particular biomolecular interactions. Con-sidering the huge number of such interactions, and their often weak and transient nature, conventional experimental methods such as X-ray crystal-lography and NMR spectroscopy are not sufficient to gain structural insight into these. A wealth of biochemical and⁄or biophysical data can, however, readily be obtained for biomolecular complexes.

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  • Placental protein 13 (PP13) was cloned from human term placenta. As sequence analyses, alignments and computa-tional modelling showed its conserved structural and func-tional homologyto members of the galectin family, the protein was designated galectin-13. Similar to human eosi-nophil Charcot–Leyden crystal protein/galectin-10 but not other galectins, its weak lysophospholipase activity was confirmed by 31 P-NMR. In this study, recombinant PP13/ galectin-13 was expressed and specific monoclonal antibody to PP13 was developed. ...

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  • Recent and increasing use of computational tools in the field of nicotinic receptors has led to the publication of several models of ligand–receptor interactions. Thesemodels are all basedon the crystal structure at 2.7 A˚ resolutionof aprotein related to the extracellular N-terminus of nicotinic acetyl-choline receptors (nAChRs), the acetylcholine binding pro-tein. In the absence of any X-ray or NMR information on nAChRs, this new structure has provided a reliable alter-native to study the nAChR structure....

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  • Toovercome the difficultyof characterizing the structures of the extracellular loops (eLPs) ofGprotein-coupledreceptors (GPCRs) other than rhodopsin, we have explored a strategy to generate a three-dimensional structural model for a GPCR, the thromboxane A2 receptor. This three-dimen-sional structurewas completedby the assembly of theNMR structures of the computation-guided constrained peptides that mimicked the extracellular loops and connected to the conserved seven transmembrane domains.

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  • The recently published novel integrinaIIbb3 ectodomain crystallographic structure and NMR structures of its transmembrane⁄cytoplasmic segments were employed to refine previously developed molecular models. Alterna-tive complete aIIbb3 models were built and evaluated, and their shape was compared with EM maps and their computed hydrodynamic⁄conforma-tional properties were compared with the available experimental data.

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  • To investigate the structural function of the C-terminal amide group of endomorphin-2 (EM2, H-Tyr-Pro-Phe-Phe-NH2), an endogenous l-opioid receptor ligand, the solution conformations of EM2 and its C-terminal free acid (EM2OH, H-Tyr-Pro-Phe-Phe-OH) in TFE (trifluoroethanol), water (pH 2.7 and 5.2), and aqueous DPC (dodecylphosphocholine) micelles (pH 3.5 and 5.2) were investigated by the combination of 2D 1 H-NMR meas-urement and molecular modelling calculation.

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  • NMR spectroscopy and X-ray crystallography have provi-ded important insight into structural features of phenyl-alanine hydroxylase (PAH) and tyrosine hydroxylase (TH). Nevertheless, significant problems such as the substrate specificity of PAHand the different susceptibility of TH to feedback inhibition by L-3,4-dihydroxyphenylalanine (L-DOPA) compared with dopamine (DA) remain unre-solved.

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  • Within the last decade the interest in lipases has increased dramatically, and no doubt, this interest will be maintained in the future. Novel and powerful tools of molecular biology, crystallography, NMR technology and molecular modeling will continue to reveal new amino acid sequences and three-dimensional structures of lipases. In addition, transgenic and knockout animal models as well as the use of specific inhibitors will add knowledge about their mode of interaction with lipid substrates, cleavage mechanism and physiological roles in humans....

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  • The temperature-induced structural transitions of the full length Alzheimer amyloid b-peptide [Ab(1–40) peptide] and fragments of it were studied using CD and 1 H NMR spectroscopy. The full length peptide undergoes an overall transition from a state with a prominent population of left-handed 31 (polyproline II; PII)-helix at 0C to a random coil state at 60C, with an averageDH of 6.8 ± 1.4 kJÆmol )1 per residue, obtained by fitting a Zimm–Bragg model to the CD data.

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