Characterizing the molecular details of stress proteins in E. coli

Molecular chaperones are a group of proteins that help cells respond to stress. While they can be extremely useful in the human body, bacteria also use chaperones to survive under stressful conditions, such as high or low temperatures, or the presence of antibiotic treatments. Given the role of chaperones in responding to cellular stress, inhibition of these chaperones represents a new strategy to slow bacterial growth and treat infections.

Recently, studies have identified important functions of a physical interaction between two types of chaperones, Hsp70s and J-domain proteins. However, these insights from human chaperones have yet to be explored in bacterial chaperones. In this project, students will use protein biochemistry to study the molecular details of a pair of E. coli chaperones. Understanding these molecular details is an important first step before drug-like molecules can be developed! Students will gain skills in protein purification, structure-guided hypothesis generation, and binding assays.

Project Duration

8 weeks (June 6-July 29)

Prerequisite Courses

CHEM 117: Chemistry

Preferred Courses


Number of Positions


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