BIOA01H3 Lecture Notes - Lecture 1: Thymine, Deoxyribose, Nitrogenous Base

• School: UTSC
• Department: Biological Sciences
• Course: BIOA01H3
• Professor: Steve Joordens

Document Summary

Result of hydrogen bonding among molecules of the amino acid backbone. H-bonding occurs between nitrogen and oxygen atoms and hydrogen atoms. Highly regular secondary structure are alpha helix and beta pleated sheet. Specific bonding arrangements between r groups give rise to a proteins distinctive 3-d shape, or conformation. Extreme conditions can unfold protein from its conformation, causing denaturation: quaternary structures some proteins are composed of two or more polypeptides that come together to form a functional protein. This structure is a level of organization that exisits in many proteins, hemoglobin for example, which contains four indicividual folded polypeptides. Bonds and forces that fold single amino acid chains into tertiary structures hold multiple polypeptide chains together. Prosthetic groups many proteins require nonprotein components called prosthetic groups in order to function. Example: hemoglobin having oxygen bound to molecules called heme. Chapter 14. 1a genes specifiy either protein or rna products.