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Laboratory Skills in Biochemistry


  • Credit value: 15 credits at Level 4
  • Convenor: Professor Carolyn Moores
  • Assessment: three sets of lab notes (10% each), a problem-solving test (5%), two data analyses (20% each) and a 1500-word scientific paper report (25%); 80% attendance required (0%)

Module description

While studying biological sciences at university you will need to think critically about evidence and acquire essential practical skills.

In this module, we build on the foundations laid in Practical Skills for the Biosciences, reinforcing the basic laboratory and generic skills already gained by introducing new contexts in which to practise these skills. You will also have the opportunity to practise skills gained in the preceding module, Quantitative Skills and Experimental Design. Further, we will introduce new topic areas and new laboratory techniques, expanding your overall laboratory skills 'tool set'.

Overall, the three modules will prepare you for more advanced lab work in molecular biology and protein biochemistry at Levels 5 and 6.

Indicative syllabus

  • Principles of enzymatic catalysis
    • Applications: conducting in vitro enzyme assays; analysing and interpreting data derived from enzyme assays
  • Principles of liquid column chromatography
    • Applications: ion exchange and affinity chromatography
  • Principles of electrophoresis as applied to protein samples
    • Applications: separation and visualisation of proteins by SDS-PAGE; estimation of the sizes of proteins from SDS-PAGE results; electroblotting of SDS polyacrylamide gels
  • Principles of immunoassays
    • Applications: western blotting

Learning objectives

By the end of this module, you will be able to:

  • show mastery of all the learning outcomes expressed in Practical Skills for the Biosciences
  • prepare slides for optical light microscopy and correctly identify specific features in a blood smear
  • determine the total concentration of protein in a supplied sample
  • enumerate the principles underpinning selected modes of liquid chromatography and use these to explain how protein separations can be achieved using the selected techniques
  • quantitatively account for the recovery of proteins following a chromatographic separation
  • enumerate and explain the principles underpinning protein separation by SDS-polyacrylamide gel electrophoresis (SDS-PAGE)
  • use SDS-PAGE to separate proteins in a sample by their size; subsequently to stain a gel to visualise the proteins; and to determine the sizes of previously uncharacterised proteins, observed in a gel, by comparison to standards of known size
  • explain the principles underpinning immunodetection of proteins and use western blotting/immunodetection to confirm the presence of a specific protein in an electrophoresed sample
  • make decisions based on preliminary data on how best to monitor the activity of an enzyme in an in vitro assay
  • express enzyme activity in various ways, interconvert these expressions as needed, and compute descriptive statistics relevant to analysis of enzyme assay data
  • identify key parameters influencing (1) the progress of an enzyme-catalysed reaction in vitro, and (2) the rate of an enzyme catalysed reaction in vitro and provide detailed explanations in each case
  • present and evaluate laboratory findings in writing, following a professional scientific paper format.