COVID-19 - UPDATE 3.4.2020: It is with considerable regret that we announce the cancellation of this course for 2020 but it will be rescheduled to 2021. We are closely monitoring the COVID-19 situation as it evolves, following CDC guidelines to ensure the safety and well-being of our participants and staff. Participants from CDC Warning Level 3 countries (currently China, South Korea and Italy) are being advised to cancel their participation at upcoming courses unless they can demonstrate having departed the area at least two weeks prior to their visit to CSHL. We are evaluating our future events on a four-week rolling basis. Full advisory
See the roll of honor - who's taken the course in the past
This course is for scientists, including graduate students, postdoctoral scholars, staff scientists, and principal investigators, who want a rigorous introduction to expression and purification of proteins as well as analysis of protein structure and function.
Through hands-on experience in the lab as well as extensive lecture and discussion, each student will become familiar with key approaches in expression, purification, and analysis of soluble and membrane proteins and protein complexes from both natural sources and overexpression systems.
The emphasis of the course is on the following:
- Approaches in protein expression: Choosing the best bacterial or eukaryotic expression system tailored for the particular protein and experimental problem; determining how to optimize expression; understanding protein tagging: the advantages and pitfalls of various affinity and solubility tags.
- Approaches in protein purification: Choosing the best strategy for a given protein including solubilization; bulk fractionation; liquid chromatography: including conventional methods (ion exchange, size exclusion, reverse phase, etc.) and affinity methods (e.g., MAC, DNA affinity, immunoaffinity, etc.), as well as FPLC/HPLC.
- Approaches in protein analysis: introduction to common approaches for characterization of proteins including binding assays; activity assays; mass spectroscopy to identify protein interaction partners and post-translational modifications.
In addition to purification, students will also gain exposure to fundamental analytical approaches such as mass spectroscopy and protein structure determination (e.g., X-ray crystallography, cryo-EM, etc.).
Andrew Quigley, Diamond Light Source, United Kingdom Darryl Pappin,
Jiansen Jiang, National Institutes of Health
Donald Jarvis, University of Wyoming
Cold Spring Harbor Laboratory
This course is supported by: National Cancer Institute
Financial aid is available to offset tuition costs as follows:
Please indicate your eligibility for funding in your financial aid request submitted as part of your application materials. Financial aid requests do not affect selection decisions made by the instructors.
We would like to acknowledge the following companies that provided invaluable support
Lab Equipment: Bio-Rad Laboratories, GE Healthcare Corp., Waters
Cost (includes food and housing): $4,080
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 5 PM on March 24 and to depart any time on April 6.
Before applying, ensure you have:
- Personal statement/essay;
- Letter(s) of recommendation;
- Curriculum vitae/resume (optional);
- Financial aid request (optional).
If you are not ready to fully apply but wish to express interest in applying, receive a reminder two weeks prior to the deadline, and tell us about your financial aid requirements, click below:
For more on this course, read
what former trainees said of their experiences. Also, be sure to check out
the growing online alumni presence.