| CODE | PHB1502 | ||||||||||||||||
| TITLE | Protein Chemistry and Enzymology | ||||||||||||||||
| UM LEVEL | 01 - Year 1 in Modular Undergraduate Course | ||||||||||||||||
| MQF LEVEL | 5 | ||||||||||||||||
| ECTS CREDITS | 6 | ||||||||||||||||
| DEPARTMENT | Physiology and Biochemistry | ||||||||||||||||
| DESCRIPTION | This study-unit provides a description and analysis of protein chemistry, relating protein structure to function of different classes of proteins, highlighting the relevance of protein in both health and disease. Emphasis is given to the physical properties of proteins and their application to experimentation techniques. Study-unit Aims: This study-unit aims to teach students about the: - Structure-function relationship of different classes of proteins; - Importance of structures of proteins to the function of different classes of proteins; - Different enzyme classes; - Mechanism of catalysis of basic reactions; - Different enzyme kinetics. Learning Outcomes: 1. Knowledge & Understanding: By the end of the study-unit the student will be able to: - Characterise proteins by primary, secondary, tertiary and quaternary structure; - Explain the difference between motifs and domains in proteins; - Correlate protein structure with protein function; - Describe the role of non-protein components of proteins; - Describe the post-translational modifications of protein and the effect these have on protein function; - Explain the pathways of protein folding and refolding and their involvement in the mechanism of disease; - Describe the structure, assembly and function of fibrous protein, elastin and collagen; - Discuss ligand binding to proteins; - Compare and contrast the chemical, structural and functional properties of haemoglobin and myoglobin; - Describe enzyme kinetics; - List the different types of reversible enzyme inhibition, along with examples of each form; - Describe irreversible enzyme inhibition, together with examples highlighting their pharmaceutical importance; - Describe the mechanisms of catalysis in enzymes; and - Describe in detail the catalysis of chymotypsin, ribonuclease, aspartyl transcarbamoylase and lysozyme. 2. Skills: By the end of the study-unit the student will be able to: - Perform laboratory techniques; including purification, quantification and analysis of proteins; - Apply the Michaelis Menten equation; - Derive the Lineweaver-Burke equation; - Prepare a standard calibration; - Use a spectrophotometer; - Separate proteins by electrophoresis; - Scale up protein production for industry; - Interpret analytical data; - Design an experiment involving protein purification; - Design an experiment to study the effect of a protein inhibitor; - Associate aberrant protein function with disease; - Distinguish between therapeutic inhibitors and activators of enzymes; and - Research and present scientific information in the form of a seminar. Main Text/s and any supplementary readings: Main Text: Nelson, D. L. and Cox, M. M.. Lehninger Principles of Biochemistry. 6th edition. New York, Worth Publishers. 2013. Supplementary Reading: Watson, D. J., Baker, T, A., Gann, A., Levine, M. and Losick, R. Molecular Biology of the Gene. 7th edition. New York: Cold Spring Harbor Press. 2013. |
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| STUDY-UNIT TYPE | Lecture, Independent Study, Practical & Seminar | ||||||||||||||||
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The University makes every effort to ensure that the published Courses Plans, Programmes of Study and Study-Unit information are complete and up-to-date at the time of publication. The University reserves the right to make changes in case errors are detected after publication.
The availability of optional units may be subject to timetabling constraints. Units not attracting a sufficient number of registrations may be withdrawn without notice. It should be noted that all the information in the description above applies to study-units available during the academic year 2024/5. It may be subject to change in subsequent years. |
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