CAS BI 525 Lecture Notes - Lecture 3: Beta Sheet, Post-Translational Modification, Alpha Helix
1 Oct 2016
School
Department
Course
Professor
Document Summary
Changing a domain that should not be beta sheet to beta sheet. Beta sheet bonds- hydrogen bonds same chemical bonds as alpha helix. Planar position that gives the molecule the possibility to make bonds with amino acids on a parallel plane. Beta sheet is considered the abnormal confirmation when the protein is turned to beta sheet. Methods of doing this: phosphorylation, cleavage/proteolysis, ph, metal chelation (changes in the cell) Factors that might influence protein denaturation and misfolding: mutations, glucose levels, oxidation, changes in physiological ph, binding to ions, levels/concentration of monomers: if low the proteins tends not to aggregates, if high the protein tends to form aggregates. Post-translational modifications happen secondary to the changes in the cell leads to permanent change to abnormal conformation. Then intermolecular forces/contacts (hydrogen bonds) between multiple abnormal conformation lead to globular intermediates (oligomers), protofibrils, fibers, and plaques/inclusions. Globular intermediates= oligomers (cannot be visualized, can be detected biochemically)
