INSTRUCTIONS - PROFESSORS: Please print and review this form. Complete or correct the sections, as applicable, from "Supervisor's Name" to "Ethics, safety, and training". Please sign and date near the bottom ("Supervisor's signature").
INSTRUCTIONS - STUDENTS: You may receive this form by email, or you may simply print this webpage. Either way, print and review this form. Complete or correct the sections, from "Student's Name" to "Student's Level", and sign ("Student signature"). Ask your supervisor to sign her/his section near the bottom. Take it to the department* corresponding to the course number in Section A; this may or may not be your own department. (* EXCEPTIONS: For NSCI 396 and COGS 396, please bring it to the Interdisciplinary Programs Adviser in Dawson Hall.) Do not register for a '396' course on Minerva until you receive departmental permission. Have a discussion with your supervisor about time/work expectations, keeping in mind that this is a 3-credit course (roughly, 10 hours per week for 12 weeks). Remember that a '396' course is an elective.
INSTRUCTIONS - DEPARTMENTS: After the unit chair/director/designate approves (or not) this project, please notify student. If approved, please give student permission to register on Minerva, and send a copy of this form (with signatures) to the Office for Undergraduate Research in Science (either fax, or internal mail to Dawson Hall 408-A, or PDF scan + email).
QUESTIONS OR FEEDBACK? Contact the Office for Undergraduate Research in Science.
Supervisor's Name: Jason Young
Supervisor's Email: jason [dot] young2 [at] mcgill [dot] ca
Supervisor's Phone: 2006
Supervisor's department: Biochemistry
Course number: BIOC 396 (Biochemistry)
Term: Fall 2013-2014
Project start date: Tuesday, September 3, 2013
Project end date: Tuesday, December 3, 2013
Project title: Mechanism of chaperone-assisted folding by Hsp70 and DNAJA2
Project description (50-100 words suggested): Hsp70, a key human chaperone, assists folding through ATP-driven cycles of substrate polypeptide binding. Hsp70-mediated folding requires specific co-chaperones, such as DNAJA2. DNAJA2 activates Hsp70 to hydrolyze ATP, simultaneously transfering substrate from itself onto Hsp70. Homology modeling of DNAJA2 identified highly conserved surface exposed residues, the functions of which are unknown. These residues will be point mutated and we will use our established methods to study DNAJA2 function in cells and as a pure protein. DNAJA2 mechanisms will be compared with a putative Hsp70 inhibitor and if necessary, mutants of Hsp70.
Prerequisite: 1 term completed at McGill + CGPA of 3.0 or higher; or permission of instructor.
Grading scheme (The final report must be worth at least 50% of final grade): 50% report, 50% performance.
Project status: This project is taken; however students may contact the professor to discuss other possible '396' projects this term.
Ethics, safety, and training: Supervisors are responsible for the ethics and safety compliance of undergraduate students. This project involves NEITHER animal subjects, nor human subjects, nor biohazardous substances, nor radioactive materials, nor handling chemicals, nor using lasers.