Cellular Functions
Cellular Functions
CORE TOPIC 1: CELLULAR FUNCTIONS
Learning Outcomes: (a) Describe and interpret drawings and photographs of typical animal and plant cells as seen under the electron microscope, recognising the following membrane systems and organelles: rough and smooth endoplasmic reticulum, Golgi body, mitochondria, ribosomes, lysosomes, chloroplasts, cell surface membrane, nuclear envelope, centrioles, nucleus and nucleolus. (b) Outline the functions of the membrane systems and organelles listed in (a). (c) Describe the formation and breakage of a glycosidic bond. (d) Analyse the molecular structure of a triglyceride and a phospholipid, and relate these structures to their functions in living organisms. (e) Describe the structure of an amino acid and the formation and breakage of a peptide bond. (f) Explain the meaning of the terms primary structure, secondary structure, tertiary structure and quaternary structure of proteins, and describe the types of bonding (hydrogen, ionic, disulfide and hydrophobic interactions) which hold the molecule in shape. (g) Analyse the molecular structure of a dimeric enzyme with a quaternary structure e.g. viral/HIV protease, as an example of a globular protein, and of collagen as an example of a fibrous protein, and relate these structures to their functions. (h) Explain the mode of action of enzymes in terms of an active site, enzyme/substrate complex, lowering of activation energy and enzyme specificity. (i) Follow the time course of an enzyme-catalysed reaction by measuring rates of formation of products (e.g. using catalase) or rate of disappearance of substrate (e.g. using amylase). (j) Investigate and explain the effects of temperature, pH, enzyme concentration and substrate concentration on the rate of enzyme catalysed reactions, and explain these effects. (k) Explain the effects of competitive and non-competitive inhibitors on the rate of enzyme activity. (l) Explain the importance of mitosis in growth, repair and
CORE TOPIC 1: CELLULAR FUNCTIONS
Learning Outcomes: (a) Describe and interpret drawings and photographs of typical animal and plant cells as seen under the electron microscope, recognising the following membrane systems and organelles: rough and smooth endoplasmic reticulum, Golgi body, mitochondria, ribosomes, lysosomes, chloroplasts, cell surface membrane, nuclear envelope, centrioles, nucleus and nucleolus. (b) Outline the functions of the membrane systems and organelles listed in (a). (c) Describe the formation and breakage of a glycosidic bond. (d) Analyse the molecular structure of a triglyceride and a phospholipid, and relate these structures to their functions in living organisms. (e) Describe the structure of an amino acid and the formation and breakage of a peptide bond. (f) Explain the meaning of the terms primary structure, secondary structure, tertiary structure and quaternary structure of proteins, and describe the types of bonding (hydrogen, ionic, disulfide and hydrophobic interactions) which hold the molecule in shape. (g) Analyse the molecular structure of a dimeric enzyme with a quaternary structure e.g. viral/HIV protease, as an example of a globular protein, and of collagen as an example of a fibrous protein, and relate these structures to their functions. (h) Explain the mode of action of enzymes in terms of an active site, enzyme/substrate complex, lowering of activation energy and enzyme specificity. (i) Follow the time course of an enzyme-catalysed reaction by measuring rates of formation of products (e.g. using catalase) or rate of disappearance of substrate (e.g. using amylase). (j) Investigate and explain the effects of temperature, pH, enzyme concentration and substrate concentration on the rate of enzyme catalysed reactions, and explain these effects. (k) Explain the effects of competitive and non-competitive inhibitors on the rate of enzyme activity. (l) Explain the importance of mitosis in growth, repair and