Waters Webinars

Waters, a Sponsor of WBMSDG, is offering a comprehensive list of free LIVE Webinars and Ask the Expert sessions.

Topics include Empower, HPLC/UPLC, Mass Spectrometry, MassLynx, UNIFI, and due to the current circumstances of Covid 19, long term shutdown procedures for Waters LC and MS Systems. Registration for these sessions can be completed using the following link at Waters Customer Education (The Promo Code for these classes is 2020WEB and this should be entered in the purchase order field). Waters will be adding additional courses throughout the April and May so check back often!

Waters also has a number of other free online resources available including webinars, fundamentals of LC/MS, how-to-videos, information on managing data, and more. Please use the following link to learn more. Starting April 8th, please join Waters for STEM Live: The Science of What’s Possible for Kids, a new weekly series, where Waters will bring fun experiments for all ages into your home laboratories.

April 2020 Virtual Meeting

Speaker: Ben Neely, NIST

Topic: Sea lions and bats and humans, oh my! How to explore mammalian serum proteomes

Date: Monday, April 20th, 2020

NEW TIME: 1:00 pm Presentation

Location: Webinar – see email on April 16 for invite link. Join the mailing list

Abstract: Comparative biology and biomimicry are broadly focused on understanding the underlying molecular basis of phenotypes relevant to chronic human ailments. Notably, research in hibernating mammals is improving our understanding of neurodegeneration, studies of diving mammals is identifying novel mechanisms of ischemia/reperfusion injury resistance, while studying organisms that follow Peto’s paradox is advancing longevity and cancer research. In addition to biomimetics, recent events are highlighting certain mammal’s ability to serve as reservoirs of infectious disease. Systematically characterizing the diversity of all mammalian proteomes will enable unexpected discoveries, but this presents numerous technological hurdles. In this seminar I will present results, recommendations and solutions to the issues of working in species without genomes or annotations, acquiring proteomic data in a standardized fashion, comparing proteomes between species and identifying molecular trends across clades with relevant phenotypes. Using the Atlantic bottlenose dolphin and California sea lion as examples, I will demonstrate improvements in proteomic analysis using genomic sequencing and gene annotation techniques, as well as emerging proteomic techniques such as data-independent acquisition applied to undepleted human and bat serum.

CANCELLED: March 2020 Meeting

Speaker: Carlos Larriba-Andaluz, Purdue School of Engineering & Technology

Topic: Understanding Ion Mobility Separation in High-Resolution Instruments. Caveats of and deviations from the Mason-Schamp Equation for small molecules.

Look for this talk to be re-scheduled in the future!

3rd Annual North American Mass Spectrometry Summer School

June 15 – 18, Madison, WI

Join us for our third annual mass spectrometry summer school. We are proud to have assembled over a dozen world leading experts in mass spectrometry for this four-day course. Our goal is to provide our students, both from academia and industry, an engaging and inspiring program covering the latest in the application of mass spectrometry to omic analyses. Tutorial lectures range from mass analyzers to the basics of data analysis. Also planned are several hands-on workshops – aimed at both scientific and professional development. This program is made possible by generous funding from the National Science Foundation (Integrated Organismal Systems, Plant Genome Research Program, Grant No. 1546742) and the National Institutes of Health National Center for Quantitative Biology of Complex Systems (P41 GM108538). As such, there is no cost to participate.

Registration open through March 1, 2020: https://www.ncqbcs.com/resources/training/summer-school.

Tutorial Lectures:
Mass analyzers
Ionization
Tandem MS
Data acquisition
Quantification
Experimental design
Separations
PTMs
Metabolomics
Top-down/Native MS
Lipidomics

Hands-on Workshops:
Mass analyzers
Spectral interpretation
Publishing and reviewing
Science writing
Science illustrations

To view this discussion on the web visit https://groups.google.com/d/msgid/mass-spec-summer-school/af93b8ab-3103-4d5e-ac46-7751925ebaf6%40googlegroups.com.

February 2020 Meeting

Speaker: Casey Daniels, NIH NIAID

Topic: The dynamic ADP-ribosylome, phosphoproteome, and interactome in LPS-activated macrophages

Date: Monday, February 10th, 2020

Time: 6:15 pm Dinner, 7:15 pm Presentation

Location: Shimadzu Scientific Instruments, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)

Dinner: Please RSVP to Meghan Burke (meghan.burke@nist.gov) by Friday, February 7th if you will be attending the dinner.

Abstract: The innate immune response relies on efficient, robust, and controlled protein signaling networks to relay information related to pathogen or viral detection. This communication is mediated primarily through protein-protein interactions and post-translational modifications (PTMs), events which are best characterized by mass spectrometry (MS)-based proteomics. This in-depth study uses MS to identify changes in protein signaling networks of lipopolysaccharide (LPS)-stimulated human and mouse macrophages, at the level of single PTMs and protein complexes. Protein ADP-ribosylation is truncated down to its phosphoribose attachment structure, allowing for enrichment of the resulting phosphoribosylated peptides along with co-occurring phoshopeptides by immobilized metal affinity chromatography. Additionally, size exclusion chromatography-MS (SEC-MS) is used to separate protein complexes and proteoforms based on size; known and novel protein complexes are then identified by weighted correlation network analysis (WGCNA) – a machine learning algorithm for unsupervised clustering into modules – based on their correlated movement into or out of SEC fractions following LPS stimulation. It is only after unsupervised clustering has been performed that established databases are used to characterize the protein modules, which prove to be highly interactive based on known protein-protein interactions, and of similar biological processes, molecular functions, and/or cellular compartments based on gene ontology. Two modules of interest – one linked to the ASK complex, the other containing PARP9 as a hub protein – are studied further through immunoprecipitation and PTM analysis. Finally, PARP inhibition is used to perturb the characterized systems, demonstrating the importance of protein ADP-ribosylation for the global protein interactome. All PTM and interactome data has been aggregated into a meta-database of 6,729 proteins, with ADP-ribosylation characterized on 2,905 proteins, and phosphorylation characterized on 2,669 proteins; expanding the number of proteins with endogenous ADP-ribosylation sites characterized, identifying ADP-ribosylation in primary human cells for the first time, and surveying protein phosphorylation in human macrophages for the first time. This database serves as an invaluable resource for studying crosstalk between the ADP-ribosylome, phosphoproteome, and interactome.