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pro vyhledávání: '"Mary S. Weir"'
Autor:
Steven A. Hofstadler, Andrew Proctor, Gordon A. Anderson, Alan L. Rockwood, Qinyuan Wu, Mary S. Weir-Lipton, David C. Muddiman, Baoming M. Huang, Richard D. Smith
Publikováno v:
Journal of Chromatography A. 771:1-7
The algorithm of sequential paired covariance (SPC) has been previously reported to dramatically enhance the signal-to-noise (S/N) ratio for on-line separations combined with mass spectrometry. That initial study focused on a limited number of data s
Autor:
R. Bruce Dunlap, Mary S. Weir
Publikováno v:
Nucleosides and Nucleotides. 13:275-292
The objective of this investigation was to study the effect of pH on the dissociation constants and binding ratios of covalent complexes of thymidylate synthases from Escherichia coli and Lactobacillus casei.
Autor:
R. Bruce Dunlap, Jerome D. Odom, Ralph J. Cisneros, Mary S. Weir, Jeffrey O. Boles, J. E. Villafranca
Publikováno v:
Biochemistry. 30:11073-11080
Replacement of methionine (Met) residues by selenomethionine (SeMet) was recently shown to facilitate the crystallographic analysis of protein structure through the application of multi-wavelength anomalous diffraction techniques [Yang et al. (1990)
Autor:
Susan L, Havre, Mudita, Singhal, Deborah A, Payne, Mary S Weir, Lipton, Bobbie-Jo M, Webb-Robertson
Publikováno v:
IEEE engineering in medicine and biology magazine : the quarterly magazine of the Engineering in MedicineBiology Society. 24(3)
Proteins play a key role in cellular processes, making proteomics central to understanding systems biology. MS techniques provide a means to observe entire proteomes at a global level. Yet, high-throughput MS proteomics techniques generate data faste
Publisher Summary This chapter explores the characterization of the natural and radiation-induced modification of histones. It highlights the feasibility of analyzing both natural and induced modifications of histone proteins by ESI–MS. In the mode
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9165b848508cb8861a95e79aabdc85c6
https://doi.org/10.1016/b978-0-12-194710-1.50018-7
https://doi.org/10.1016/b978-0-12-194710-1.50018-7
Publikováno v:
Biochemistry. 32(36)
The recent determination of the crystal structure of Escherichia coli thymidylate synthase (TS) [Matthews et al. (1989) J. Mol. Biol. 205, 449-454] has implicated the glutamic acid residue at position 58 in a mechanistic role which could involve the
Autor:
Havre, Susan L., Singhal, Mudita, Payne, Deborah A., Lipton, Mary S. Weir, Webb-Robertson, Bobbie-Jo M.
Publikováno v:
IEEE Engineering in Medicine & Biology Magazine; May/Jun2005, Vol. 24 Issue 3, p50-57, 8p, 8 Color Photographs, 5 Black and White Photographs, 2 Diagrams
Publikováno v:
Rapid Communications in Mass Spectrometry; October 1997, Vol. 11 Issue: 15 p1673-1676, 4p