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Learn the basic structure of amino acids, peptide bonds, and the molecular structure of haemoglobin. Discover the roles of proteins, from structural to catalytic functions, and the levels of protein structure. Explore the bonds involved in protein formation and maintenance.
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Haemoglobin: Structure and Formation of Proteins 1.1.2, a, b,c
Learning Objectives • Describe, with the aid of diagrams, the basic structure of an amino acid. (D) • Describe, with the aid of diagrams, the condensation reaction between two amino acids to form a peptide bond. (C) • outline the molecular structure of haemoglobin as an example of a globular protein, including the meaning of the following terms: primary structure, secondary structure, tertiary structure, quaternary structure and prosthetic group. (B)
Starter • What is digestion? • Write the word equation for protein digestion. • What do you think will happen to build up protein molecules?
Introducing proteins Proteins are a diverse group of large and complex polymer molecules, made up of long chains of amino acids. They have a wide range of biological roles, including: structural: proteins are the main component of body tissues, such as muscle, skin, ligaments and hair catalytic: all enzymes are proteins, catalyzing many biochemical reactions signalling: many hormones and receptors are proteins immunological: all antibodies are proteins.
aminogroup carboxylic acid group R group The general structure of amino acids All amino acids have the same general structure: the only difference between each one is the nature of the R group. The R group therefore defines an amino acid. The R group represents a side chain from the central ‘alpha’ carbon atom, and can be anything from a simple hydrogen atom to a more complex ring structure.
Polypeptides When more amino acids are added to a dipeptide, a polypeptide chain is formed. A protein consists of one or more polypeptide chains folded into a highly specific 3D shape. There are up to four levels of structure in a protein: primary, secondary, tertiary and quaternary. Each of these play an important role in the overall structure and function of the protein.
hydrogen bonds:involved in all levels of structure. hydrophobic interactions:between non-polar sections of the protein. disulfide bonds: one of the strongest and most important type of bond in proteins. Occur between two cysteine amino acids. Bonds in proteins The 3D shape of a protein is maintained by several types of bond, including:
Task Answer questions 1and 2. page 13
Homework Write an essay to explain the difference between globular and fibrous proteins that includes: • Definition. • Explaining the function • Example/s • Explain some blood disorder, for example: beta thalassaemia, glycosylated haemoglobin and sickle cell anaemia. Use your books and the website for details. Due next Wednesday