Zobrazeno 1 - 10
of 114
pro vyhledávání: '"Michael L. Gross"'
Publikováno v:
J Am Soc Mass Spectrom
Protein glycosylation is a common and highly heterogeneous post-translational modification that challenges biophysical characterization technologies. The heterogeneity of glycoproteins makes their structural analysis difficult; in particular, hydroge
Publikováno v:
J Am Soc Mass Spectrom
Synchrotron radiolysis generates hydroxyl radicals (•OH) that are successful footprinting reagents. Here, we describe a new reagent for the synchrotron platform, the trifluoromethyl radical (•CF(3)). The radical is produced by •OH displacement
Autor:
Ke Sherry Li, Brett R. Beno, Ekaterina G. Deyanova, Richard Y.-C. Huang, Michael L. Gross, Elizabeth T. Schaper Bergman, Guodong Chen
Publikováno v:
J Am Soc Mass Spectrom
Mass spectrometry (MS)-based protein footprinting, a valuable structural tool in mapping protein-ligand interaction, has been extensively applied to protein-protein complexes, showing success in mapping large interfaces. Here, we utilized an integrat
Publikováno v:
J Am Soc Mass Spectrom
Membrane proteins play crucial roles in cell signaling and transport and, thus, are the targets of many small molecule drugs. The characterization of membrane protein structures poses challenges for the high-resolution biophysical tools because the t
Publikováno v:
Journal of the American Society for Mass Spectrometry. 30:213-217
We report a novel method named LITPOMS (ligand titration, fast photochemical oxidation of proteins and mass spectrometry) to characterize protein-ligand binding stoichiometry, binding sites, and site-specific binding constants. The system used to tes
Autor:
Michael L. Gross, Weidong Cui, Ben Niu, C. Robert Matthews, Don L. Rempel, Brian C. Mackness, Hao Zhang, Jill A. Zitzewitz
Publikováno v:
Journal of the American Society for Mass Spectrometry. 28:389-392
Incorporation of a reporter peptide in solutions submitted to fast photochemical oxidation of proteins (FPOP) allows for the correction of adventitious scavengers and enables the normalization and comparison of time-dependent results. Reporters will
Autor:
Hanliu Wang, Brandon T. Ruotolo, Hao Zhang, Carl Frieden, Michael L. Gross, Joseph D. Eschweiler, Weidong Cui
Publikováno v:
J Am Soc Mass Spectrom
Apolipoprotein E (apoE) is an essential protein in lipid and cholesterol metabolism. Although the three common isoforms in humans differ only at two sites, their consequences in Alzheimer’s disease (AD) are dramatically different: only the e4 allel
Autor:
Mindy Prado, Don L. Rempel, Yue Lu, Michael L. Gross, Hao Zhang, Lucas B. Harrington, Rafael G. Saer, Robert E. Blankenship
Publikováno v:
Journal of the American Society for Mass Spectrometry. 28:87-95
Native mass spectrometry (MS) is an emerging approach to study protein complexes in their near-native states and to elucidate their stoichiometry and topology. Here, we report a native MS study of the membrane-embedded reaction center (RC) protein co
Autor:
Aaron T. Wecksler, Michael L. Gross, Patricia Molina, Weidong Cui, Galahad Deperalta, Ying Zhang, Hao Zhang
Publikováno v:
Journal of the American Society for Mass Spectrometry. 27:1139-1142
Native mass spectrometry (MS) and top-down electron-capture dissociation (ECD) combine as a powerful approach for characterizing large proteins and protein assemblies. Here we report their use to study an antibody Fab (Fab-1)-VEGF complex in its near
Publikováno v:
Journal of the American Society for Mass Spectrometry. 27:178-181
We report an isotope-encoding method coupled with carboxyl-group footprinting to monitor protein conformational changes. The carboxyl groups of aspartic/glutamic acids and of the C-terminus of proteins can serve as reporters for protein conformationa