July 14 - 27, 2015
Application Deadline: March 31, 2015
Michael Bereman, North Carolina State University Michelle Cilia, Cornell University
Ileana Cristea, Princeton University Darryl Pappin, Cold Spring Harbor Laboratory
See the roll of honor - who's taken the course in the past
This intensive laboratory and lecture course will focus on cutting-edge proteomic approaches and technologies. Students will gain practical experience purifying and identifying protein complexes and posttranslational modifications. In a section focused on quantitative whole proteome analyses or top-down proteomics, students will gain hands-on experience using two-dimensional gel electrophoresis and mass spectrometry analysis. Students will use differential in-gel electrophoresis (DIGE) for gel-based protein quantification. Differentially expressed proteins will be recognized by statistical methods using advanced gel analysis software and identified using MALDI mass spectrometry. For shotgun proteomic analysis sections or bottom-up proteomics, students will use label-free and covalent isotopic-labeling quantitative approaches to differentially profile changes in protein complexes and whole proteomes. Students will be trained in high-sensitivity microcapillary liquid chromatography coupled with nanospray-ESI and tandem mass spectrometry analysis. Students will learn both single-dimension and multidimensional separation methods. In a section focused on targeted proteomics, students will learn to analyze and process shotgun proteomic data for the development of SRM/MRM assays that accurately identify and quantify targeted proteins. Students will design transitions for selected peptides and perform SRM/MRM mass spectrometry assays. They will learn to process and interpret the acquired data to measure changing quantities of targeted proteins in a variety of biological samples. For all sections of the course, a strong emphasis will be placed on data analysis.
A series of outside lecturers will discuss various proteomics topics including: imaging by mass spectrometry, de novo sequence analysis, advanced mass spectrometry methods, protein arrays, and functional proteomics. The aim of the course is to provide each student with the fundamental knowledge and hands-on experience necessary for performing and analyzing proteomic experiments. The overall goal is to train students to identify new opportunities and applications for proteomic approaches in their biological research.
Last year students used and received hands-on training on Agilent QTOF and Thermo Orbitrap, Q-exactive and Vantage triple quadrupole, and Waters SYNAPT G2-S mass spectrometers.
Speakers from 2014 included:
Karl Clauser, Broad Institute, MIT & Harvard
Frank Conlon, University of North Carolina, Chapel Hill
Michael MacCoss, University of Washington
Katalin Medzihradszky, University of California, San Francisco
David Muddiman, North Carolina State University
Alexey Nesvizhskii, University of Michigan
This course is supported with funds provided by the National Institute of Child Health & Human Development
Cost (including tuition, board and lodging): $4,080
This button links to a short form which confirms your interest in the course.
No fees are due until you have completed the full application process and
are accepted into the course.
Students accepted into the course should plan to arrive by early evening on July 13 and plan to depart after lunch on July 27.