H1 Proteins slides

Proteins

Learning Outcomes 1(e)iii. Describe the structure and properties of amino acids (in proteins) 1(f)iii. Describe the formation and breakage of a peptide bond. 1(k) Explain primary structure, secondary structure, tertiary structure and quaternary structure of proteins, and describe the types of bonds that hold the molecule in shape (hydrogen, ionic, disulfide bonds and hydrophobic interactions). Pg 101

Learning Outcomes 1(l) Explain the effects of temperature and pH on protein structure. 1(m) Describe the molecular structure of the haemoglobin protein and explain how its structure relates to its function in transport Pg 101

1. Amino acids 2. Formation of peptide bonds 3. Levels of organisation in proteins A. Primary Structure B. Secondary Structure C. Tertiary Structure D. Quaternary Structure 4. Case Studies: Haemoglobin

Introduction Pro-insulin ✣Made up of the elements carbon, hydrogen & oxygen, nitrogen and sometimes sulphur ✣Building blocks of proteins are monomers called amino acids Pg 101

Functions of Proteins Collagen Ovalbumin Haemoglobin Insulin / glucagon GPCR / RTK Actin Antibodies DNA polymerases, lipase

Collagen – cartilage & tendons DNA polymerase III – DNA replication Antibody Haemoglobin

1. Amino acids 2. Formation of peptide bonds 3. Levels of organisations in proteins A. Primary Structure B. Secondary Structure C. Tertiary Structure D. Quaternary Structure 4. Case Studies: Haemoglobin

Learning Outcome 1(e)iii. Describe the structure & properties of amino acids Pg 101

Structure of an amino acid Pg 101