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  • 1
    ISSN: 1573-4943
    Keywords: Mass spectrometry ; deuterium exchange ; two-dimensional separations ; secondary structure ; protein: ligand interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract When mass spectrometry (MS) is used to study protein primary structure, it is used in a “static” mode. That is, the information is derived from a single MS or MS-MS spectrum. Information about more complex protein structure or protein interactions can also be gained via MS. If a series of mass spectra is collected as something else in the experiment is changing, we increase the “dimensionality” of the MS data. For example, measuring mass spectra as a function of time after exposure of a protein to deuterated solvents can provide information about protein structure. Likewise, by measuring mass spectra of a protein as the concentration of a binding ligand is changed, one can infer the stoichiometry of the complex. Another important, but fundamentally different way of increasing the dimensionality of mass spectral data is by coupling the mass spectrometer to a one- or two-dimensional separation technique.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Microcolumn Separations 2 (1990), S. 293-299 
    ISSN: 1040-7685
    Keywords: multidimensional separations ; two-dimensional separations ; CZE ; capillary electrophoresis ; peptide fingerprinting ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Comprehensive two-dimensional reversed-phase HPLC-capillary electrophoresis (RP HPLC-CE) was used to compare the tryptic digest fingerprints of horse heart cytochrome C and bovine heart cytochrome C. The peptide fragments were labeled with fluorescamine and detected with a fluorescence detector. The two-dimensional separation system proved to be reproducible enough to identify some species differences in the tryptic digest fingerprints. Improvements in instrumentation and daily procedures yielding faster analysis times and better reproducibility compared to a previous system are described. Improvements in software yielding gray-scale images of the two-dimensional data are described. Identification of selected tryptic fragments was achieved.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Microcolumn Separations 1 (1989), S. 41-45 
    ISSN: 1040-7685
    Keywords: capillary electrophoresis ; mobility ; diffusion coefficient ; proteins ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Capillary zone electrophoresis can be used to determine mobilities and diffusion coefficients for analytes. Mobilities are determined from measurements of migration times. Correction for electroosmotic flow must be made by measuring the flow magnitude using an uncharged marker substance. Diffusion coefficients can be measured from peak widths of analyte bands. Care must be taken in these measure- ments that the analyte concentration does not overload the system and perturb the axial homogeneity of the electric field strength. Analyte also must not adsorb to the surface of the capillary. Finally, the capillary should be operated with a power dissipation that is low enough that minimal heating of the capillary occurs. Capillary zone electro- phoresis offers some advantages over other methods of determining mobilities and diffusion coefficients. These include a requirement of only small quantities of analyte at relatively low concentrations and the capability of making measurements on several substances simultaneously in mixtures.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Microcolumn Separations 1 (1989), S. 125-130 
    ISSN: 1040-7685
    Keywords: micellar electrokinetic capillary chromatography ; capillary electrophoresis ; isotopic separations ; micellar separations ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Near-baseline resolution of dansylated methylamine and dansylated methyld3-amine can be achieved by micellar electrokinetic capillary chromatography (MECC) utilizing a 25-mM sodium dodecylsulfate pseudostationary phase and a mobile phase containing 4.9 M methanol. This study examines the role of methanol on this separa- tion by looking at its effects on to, tr,tm, and resolution over four methanol concentrations, 0 M, 2.5 M, 4.9 M, and 7.4 M. The 4.9 M methanol buffer proves to be the best for optimizing the resolution of these two extremely similar compounds. Because of the high organic content of the mobile phase, it is unreliable to determine tm based upon the migration time of a single species. A method for determining tm based upon a homologous series of standards is presented and examined over the four methanol concentrations. Plots of log k′ versus carbon number yield straight lines with similar slopes for each of the four buffer systems, indicating that this procedure is a good method for tm determination.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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