Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Binding comparison

Fox, K. M., and Karplus, P. A., 1994, Old yellow enzyme at 2.0 resolution overall structure, ligand binding, comparison with related flavoproteins. Structure 2 1089nll05. [Pg.69]

Sharp KA, Friedman RA, Misra V, Hecht J, Honig B. Salt effects on polyelectrolyte-ligand binding comparison of Poisson- 83. Boltzmann, and limiting law/counterion binding models. Biopolymers 1995 36 245-262. [Pg.1140]

The molecule is the very cornerstone of neurochemistry. LSD has allowed neuroscientists to explore brain biochemistry e.g. mental illness, serotonin receptors, serotonin receptor subtypes and numerous binding comparisons with other active molecules. Some drugs which have been found to block the effects of LSD are useful antipsychotics. Early studies described LSD as a psychotomimetic, yet this is a general term applied to all phantasmogens. [Pg.1]

Zhang LY, Gallicchio E, Friesner RA, Levy RM. Solvent models for protein-ligand binding comparison of implicit solvent Poisson and surface generalized Born models with explicit solvent simulations. J Comput Chem 2001 22 591-607. [Pg.291]

Gebbert A et al 1992 Direct observation of antibody binding. Comparison of capacitance and refractive index measurement DECHEMA Biotechnol. Conf. 1992 vol 5, part A Microbial Principles in Bioprocesses Cell Culture Technology, Downstream Processing and Recovery pp 459-62 Stenberg M et al 1979 Silicon-silicon dioxide as an electrode for electrical and ellipsometrical measurements of adsorbed organic molecules J. Colloid Interface Sci. 72 255-63... [Pg.479]

Forsten, K. E., and Lauffenburger, D. A., Interrupting autocrine ligand-receptor binding Comparison between receptor blockers and ligand decoys. Biophy. J. 63, 857 (1992b). [Pg.123]

The rates (A i) indicate pronounced amine lability, in particular piperidine, while the ratio k-i/kg suggest a strong preference for CO binding. Comparison with porphyrin and phthalocyanin complexes indicates that CO dissociation rates are relatively insensitive to the nature of the in-plane ligand unlike, those of amine dissociation k which vary from 1020 s (OMBP) to 0.50 S (phthalocyanine). The binding of CO to [Fe(TAAB)L2] + is very poor in contrast to the above results which may reflect the enormous number of differences in the structure and electronic features of TAAB relative to OMBP and other related chelates. However, CO dissociation does not occur readily, while dimethylglyoxime complexes are even more... [Pg.356]

D. Letourneau, A. Lefebvre, P. Lavigne and J.-G. LeHoux, STARD5 Specific Ligand Binding Comparison with STARDl and STARD4 Subfamilies, Mol. Cell. Endocrinol, 2013, 371, 20. [Pg.51]

K. A. Sharp, R. A. Friedman, V. Misra,J. Hecht, andB. Honig, Biopolymers, 36,245 (1995). Salt Effects on Polyelectrolyte-Ligand Binding Comparison of Poisson-Boltzmann, and Limiting Law/Counterion Binding Models. [Pg.345]

Bowler D R, Aoki M, Goringe C M, Florsfield A P and Pettifor D G 1997 A comparison of linear scaling tight-binding methods Modeiiing Simuiation Mater. Sc/. 5 199... [Pg.2229]

Figure 7-3 shows a comparison of observed binding energies with the calculated average binding energies for a few drugs. [Pg.327]

The aromatic shifts that are induced by 5.1c, 5.If and S.lg on the H-NMR spectrum of SDS, CTAB and Zn(DS)2 have been determined. Zn(DS)2 is used as a model system for Cu(DS)2, which is paramagnetic. The cjkcs and counterion binding for Cu(DS)2 and Zn(DS)2 are similar and it has been demonstrated in Chapter 2 that Zn(II) ions are also capable of coordinating to 5.1, albeit somewhat less efficiently than copper ions. Figure 5.7 shows the results of the shift measurements. For comparison purposes also the data for chalcone (5.4) have been added. This compound has almost no tendency to coordinate to transition-metal ions in aqueous solutions. From Figure 5.7 a number of conclusions can be drawn. (1) The shifts induced by 5.1c on the NMR signals of SDS and CTAB... [Pg.145]

Collins, J.B. Schleyer, P.V. Binkley, J.S. Pople, J.A. Self-consistent molecular-orbital methods. XVII. Geometries and binding energies of second-row molecules. A comparison of three basis sets J. Chem. Phys. 64 5142-5151, 1976. [Pg.110]

Fig. 4. Comparison of the three types of tetracycline resistance where T represents the tetracycline molecule O, a tetracycline transporter and aaa/, the ribosome A shows the effect of tetracycline exposure on a sensitive cell B, the efflux of resistance where a cytoplasmic membrane protein ( D) pumps tetracycline out of the cell as fast as the tetracycline transporter takes it up C, the ribosomal protection type of resistance where the ribosome is modified by ( ) to block productive binding and D, the tetracycline modification type of resistance where t is an inactive form of tetracycline. Reproduced with... Fig. 4. Comparison of the three types of tetracycline resistance where T represents the tetracycline molecule O, a tetracycline transporter and aaa/, the ribosome A shows the effect of tetracycline exposure on a sensitive cell B, the efflux of resistance where a cytoplasmic membrane protein ( D) pumps tetracycline out of the cell as fast as the tetracycline transporter takes it up C, the ribosomal protection type of resistance where the ribosome is modified by ( ) to block productive binding and D, the tetracycline modification type of resistance where t is an inactive form of tetracycline. Reproduced with...

See other pages where Binding comparison is mentioned: [Pg.39]    [Pg.226]    [Pg.424]    [Pg.73]    [Pg.546]    [Pg.1701]    [Pg.212]    [Pg.212]    [Pg.812]    [Pg.33]    [Pg.39]    [Pg.226]    [Pg.424]    [Pg.73]    [Pg.546]    [Pg.1701]    [Pg.212]    [Pg.212]    [Pg.812]    [Pg.33]    [Pg.2222]    [Pg.2843]    [Pg.168]    [Pg.139]    [Pg.608]    [Pg.110]    [Pg.726]    [Pg.82]    [Pg.146]    [Pg.108]    [Pg.177]    [Pg.219]    [Pg.220]    [Pg.237]    [Pg.444]    [Pg.276]    [Pg.283]    [Pg.173]    [Pg.140]    [Pg.312]    [Pg.171]   
See also in sourсe #XX -- [ Pg.353 , Pg.354 ]




SEARCH



Binding sites comparisons

Density-functional tight-binding function comparison

Phosphatases binding site comparison

Protein, proteins binding site comparison

© 2024 chempedia.info