'Mechanism of chaperone-assisted folding by Hsp70 and DNAJA2' - BIOC 396 Undergraduate Research Project Application Form

Supervisor's Name: Jason Young

Supervisor's Email: jason.young2 [at] mcgill.ca

Supervisor's Phone: 2006

Supervisor's Website:

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.