Zobrazeno 1 - 10
of 47
pro vyhledávání: '"Monique Laberge"'
Autor:
Carol Buettger, Pan Chen, Jane M. Vanderkooi, Ramakanth Sarabu, Bogumil Zelent, Monique Laberge, Joseph Grimsby, Franz M. Matschinsky, Stella Odili, Dorothy Zelent, Joseph Bass, Deborah Fenner, Charles A. Stanley
Publikováno v:
Biochemical Journal. 440:203-215
GK (glucokinase) is activated by glucose binding to its substrate site, is inhibited by GKRP (GK regulatory protein) and stimulated by GKAs (GK activator drugs). To explore further the mechanisms of these processes we studied pure recombinant human G
Publikováno v:
Journal of Raman Spectroscopy. 39:1848-1858
We measured the low-wavenumber polarized resonance Raman spectra of horse heart (hhc), chicken (chc) and yeastC102T (yc) ferrocytochromes c with Soret excitation. We examined the out-of-plane (oop) deformations of the heme groups by virtue of relativ
Autor:
Monique Laberge, Takashi Yonetani
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1784:1146-1158
Bohr, Hasselbalch, and Krogh discovered homotropic and heterotropic allosteric behaviors of hemoglobin (Hb) in 1903/1904. A chronological description since then of selected principal models of the allosteric mechanism of Hb, such as the Adair scheme,
Publikováno v:
Journal of Medicinal Chemistry. 51:3081-3093
We report results of 12 ns, all-atom molecular dynamics simulation (MDS) and Poisson-Boltzmann free energy calculations (PBFE) on calmodulin (CaM) bound to two molecules of trifluoperazine (TFP) and of N-(3,3, diphenylpropyl)- N'-[1- R-(3,4-bis-butox
Publikováno v:
Biophysical Journal. 92(5):1709-1716
A 3-ns molecular dynamics simulation in explicit solvent was performed to examine the inter- and intradomain motions of the two-domain enzyme yeast phosphoglycerate kinase without the presence of substrates. To elucidate contributions from individual
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764:516-521
The molecular details of the mechanism of action of allosteric effectors on hemoglobin oxygen affinity are not clearly understood. The global allostery model proposed by Yonetani et al. suggests that the binding of allosteric effectors can take place
Publikováno v:
Biopolymers. 72:241-248
Resonance Raman spectroscopy is used to probe the effect of calcium depletion on the heme group of horseradish peroxidase C at pH 8. Polarized Raman spectra are recorded with an argon ion laser at eight different wavelengths to provide a sound databa
Publikováno v:
Langmuir. 19:146-153
The effect of trehalose on the interaction of human serum albumin (HSA) with neutral and negatively charged small unilamellar vesicles (SUVs) composed of 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) or of mixtures of DMPC (19:1 w/w) with 1
Publikováno v:
Biochemistry. 40:9226-9237
Horseradish peroxidase C binds a wide variety of small H-donor compounds such as benzohydroxamic acid (BHA) and 2-naphthohydroxamic acid (NHA). In this work, we use the Mg(II)-mesoporphyrin prosthetic group derivative as a spectroscopic probe of the
Publikováno v:
International Journal of Quantum Chemistry. 84:290-301
Horseradish peroxidase C is an oxidoreductase which catalyzes in plant roots the oxidation of a remarkably wide variety of aromatic compounds by H2O2. The recently available X-ray structures of the enzyme bound to aromatic substrates are not indicati