MBB 222 Study Guide - Midterm Guide: Protein Aggregation, Fibril, Covalent Bond

• School: Simon Fraser University
• Department: Molec Biol & Biochem
• Course: MBB 222
• Professor: Adam Barlev

Document Summary

Understand that protein misfolding can cause amyloid fibril formation and lead to diseases like alzheimer"s, parkinson"s, creutzfeld-jacob (prion disease). Specific protein aggregation amyloid fibers: often the cause of disease. Amyloid: extremely insoluble fibrils that polymerize from naturally soluble protein and which are deposited in cells and tissues. Protein misfolding can cause serious human diseases; e. g. , the prion- based, creutzfeld-jacob disease (cjd) and alzheimer"s. The basic mechanism for many neurodegenerative diseases is similar and involves the formation of protein aggregates that kill nerve cells. Understand the molecular interactions that stabilize a folded protein. Tertiary folding is usually stabilized by a variety of non-covalent interactions (usually between r groups or r groups and main chains rather than h bonding between peptide bond. Know that metal ions can stabilize protein structures. Tertiary structures can be stabilized by disulfide bonds between cysteine residues or by metal ions. Know how to use dialysis to change the composition of a solution a protein is contained in.