Assessments: 2 hour examination - 65% comprising essay questions and short-answer questions. This may include some data-handling problems. Continuous assessment 35% comprising:
Practical write-up 10%
Data-handling test 20%
Molecular graphics 5% Reassessment: Supplementary examinationResit mark for the module is based solely on exam performance. Continuous assessment marks are not counted. Resit examinations will cover the whole course, i.e. theoretical aspects and practical aspects.
Learning Outcomes
By the end of the module the student should be able to:
Explain how the amino acid sequence of a protein is related to its structure and hence to its function; including simple ideas of protein evolution and common secondary structure motifs;
Describe some common protein folds and structural motifs, and relate these to the functional roles of motifs, and how the structures are stabilised.;
Evaluate techniques used to determine the primary , secondary, tertiary and quarternary structures of proteins and explain the biophysical principles behind these techniques;
Discuss the mechanisms underlying the catalysis of reactions by certain enzymes and methods used to determine enzyme rates and mechanisms;
Analyse and interpret numerical data of ligand binding, UV spectroscopy, pH and enzyme kinetics, including use of SigmaPlot;
Download, display and examine protein structure from the RSC protein database.