Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Austin Z. Salome"'
Autor:
Michael S. Westphall, Kenneth W. Lee, Austin Z. Salome, Jean M. Lodge, Timothy Grant, Joshua J. Coon
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-6 (2022)
Mass spectrometry (MS) is a powerful tool for the structural characterization of protein complexes. Here the authors offer a path for direct integration of MS and electron microscopy with a MS approach that enables grid deposition and structural pres
Externí odkaz:
https://doaj.org/article/6e45a8f643a24a1f9f34b640053ec2a6
Autor:
Jarred W. Rensvold, Evgenia Shishkova, Yuriy Sverchkov, Ian J. Miller, Arda Cetinkaya, Angela Pyle, Mateusz Manicki, Dain R. Brademan, Yasemin Alanay, Julian Raiman, Adam Jochem, Paul D. Hutchins, Sean R. Peters, Vanessa Linke, Katherine A. Overmyer, Austin Z. Salome, Alexander S. Hebert, Catherine E. Vincent, Nicholas W. Kwiecien, Matthew J. P. Rush, Michael S. Westphall, Mark Craven, Nurten A. Akarsu, Robert W. Taylor, Joshua J. Coon, David J. Pagliarini
Publikováno v:
Nature
Mitochondria are epicentres of eukaryotic metabolism and bioenergetics. Pioneering efforts in recent decades have established the core protein componentry of these organelles(1) and have linked their dysfunction to more than 150 distinct disorders(2,
Publikováno v:
Journal of proteome research.
Addressing mixtures and heterogeneity in structural biology requires approaches that can differentiate and separate structures based on mass and conformation. Mass spectrometry (MS) provides tools for measuring and isolating gas-phase ions. The devel
Publikováno v:
Analytical chemistry. 94(50)
Recently, we described the use of a chemical matrix for landing and preserving the cations of protein-protein complexes within a mass spectrometer (MS) instrument. By use of a glycerol-landing matrix, we used negative stain transmission electron micr
Publikováno v:
Organic & Biomolecular Chemistry. 19:7641-7654
Selective binding and transport of highly hydrophilic anions is ubiquitous in nature, as anion binding proteins can differentiate between similar anions with over a million-fold efficiency. While comparable selectivity has occasionally been achieved
Publikováno v:
Organicbiomolecular chemistry. 19(35)
Selective binding and transport of highly hydrophilic anions is ubiquitous in nature, as anion binding proteins can differentiate between similar anions with over a million-fold efficiency. While comparable selectivity has occasionally been achieved