MBB310 Protein Folding and Misfolding in Disease

Pre-requisites: BIS206

Aims/Description: This module examines the mechanisms employed by proteins to adopt unique functional folds and explores the causes and consequences of mis-folding, with a particular reference to neurodegenerative disease, including Alzheimer's, Parkinson's and prion diseases. Students will have an opportunity to acquire knowledge and understanding of the following: methods used to study the assembly of protein complexes; folding of molecules: background thermodynamics; folding pathways; investigating intermediates; kinetic labelling; mutagenesis; modules of folding; the role of disulphide bonds; accessory proteins; isomerases; rotamases; chaperones. Protein mis-assembly: off-pathway species, aggregation, amyloids, accessory proteins, chaperones and disaggregases. Control of protein folding and mis-folding in vivo: recognition of unfolded protein, the UPR or unfolded protein response, proteostasis, and the role of the ubiquitin-proteasome system.

Staff Contact: STANIFORTH ROSEMARY A

Teaching Methods: Lectures, Independent Study

Assessment: Formal Exam

Information on the department responsible for this unit (Molecular Biology and Biotechnology):

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Teaching timetable

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Teaching methods and assessment displayed on this page are indicative for 2021-22. Students will be informed by the academic department of any changes made necessary by the ongoing pandemic.