HTHSCI 1LL3 Lecture Notes - Lecture 7: Proline, Valine, Transmembrane Protein

• School: McMaster University
• Department: Health Sciences
• Course: HTHSCI 1LL3
• Professor: Teresa Mccurdy

Document Summary

The conformation (or shape) of a protein predicts its function - proteins held in their shape mostly by non-covalent bonds. There are several different general types of structure for proteins. Globular proteins, brous proteins, transmembrane proteins, and dna binding proteins are major classi cations for the different types. The 3d structure must be exible enough to function properly but stable enough that it will not convert to another conformation. It must have amino acids with side groups that are compatible with the environment or environments (such as a transmembrane protein) the protein will function in. So, polar groups on the outer surface if it will function in aqueous environments, hydrophobic groups in membrane insertion areas if it is a transmembrane protein. The peptide bond that forms the backbone of proteins is that between an amino group and a carboxyl group. Because of its partial double-bond characteristics the peptide bond is fairly rigid.