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7.88J / 5.48J / 7.24J / 10.543J Protein Folding Problem, Fall 2003

Protein folding factors.
Model pathway for a newly synthesized polypeptide chain emerging from the ribosome and folding to its native state, as well as an off-pathway inactive aggregated state. (Image courtesy of Professor Jonathan King.)

Highlights of this Course

The research paper and oral presentation are essential components of the course curriculum. Students must select their area of research from an extensive list of current topics in protein folding, misfolding, and their physiological roles. Topics can be found in the Projects section of this course.

Course Description

This course focuses on the mechanisms by which the amino acid sequence of polypeptide chains (proteins), determine their three-dimensional conformation. Topics in this course include sequence determinants of secondary structure, the folding of newly synthesized polypeptide chains within cells, folding intermediates aggregation and competing off-pathway reactions, and the unfolding and refolding of proteins in vitro. Additional topics covered are the role of helper proteins such as chaperonins and isomerases, protein recovery problems in the biotechnology industry, and diseases found associated with protein folding defects.
 

Staff

Instructors:
Prof. Jonathan King
Prof. David Gossard

Course Meeting Times

Lectures:
Two sessions / week
1.5 hours / session

Level

Undergraduate / Graduate

Additional Features

Translations
   Chinese (Simplified)

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