Analytical Techniques in Biochemistry

Module titleAnalytical Techniques in Biochemistry
Module codeBIO2090
Academic year2019/0
Credits15
Module staff

Dr Alison Hill (Convenor)

Duration: Term123
Duration: Weeks

11

Number students taking module (anticipated)

50

Description - summary of the module content

Module description

The distinctive features of this module are that you will learn about the ‘state of the art’ techniques that are used to look at the structure and properties of proteins and their complexes. You will have the opportunity to put your knowledge into practice during two 6 hour and one 3 hour sessions in the practical laboratory. You will gain ‘hands on’ experience in data handling and writing of scientific practical reports. This will be invaluable to you for carrying out a practical project in your final year and if you wish to continue with postgraduate studies such as a Masters or PhD. The module will also be a route to interdisciplinary studies since a general understanding of the chemistry involved in protein mechanism and the physical principles behind some methods of analysis will be acquired as part of this module.

Module aims - intentions of the module

The module will introduce you to the main experimental techniques used in the purification and characterisation of biological macromolecules, with the main emphasis on protein methodologies. It will provide you with laboratory training in selected techniques as part of experimental investigations. It will provide you with important skills of analysis of experimental data and scientific report writing. It will involve research-enriched learning in the area of protein structural and biochemical analysis, and it will provide important skills required for any future laboratory based employment opportunities.

Intended Learning Outcomes (ILOs)

ILO: Module-specific skills

On successfully completing the module you will be able to...

  • 1. Explain the principles of the bio-analytical techniques covered and have an awareness of the applications of these techniques in biochemical research
  • 2. Use selected techniques to purify proteins and analyse the success of their purification
  • 3. Characterise various properties of the purified proteins – molecular weight, enzymatic activity
  • 4. Interpret experimental data obtained using the techniques above

ILO: Discipline-specific skills

On successfully completing the module you will be able to...

  • 5. Describe and evaluate approaches to our understanding of biochemistry with reference to primary literature, reviews and research articles
  • 6. Describe in some detail essential facts and theory across a subdiscipline of the biosciences
  • 7. Identify critical questions from the literature and synthesise research-informed examples from the literature into written work
  • 8. With some guidance, deploy established techniques of analysis, practical investigation and enquiry within the biosciences

ILO: Personal and key skills

On successfully completing the module you will be able to...

  • 9. Communicate ideas, principles and theories fluently by written, oral and visual means in a manner appropriate to the intended audience
  • 10. Develop, with some guidance, a logical and reasoned argument with valid conclusions
  • 11. Collect and interpret appropriate data and complete research-like tasks, drawing on a range of sources, with limited guidance
  • 12. Work in a small team and deal proficiently with the issues that teamwork requires (i.e. communication, motivation, decision-making, awareness, responsibility, and management skills, including setting and working to deadlines)

Syllabus plan

Syllabus plan

The focus of the module is on methods of experimentation. Topics covered will include:

pH and buffers, centrifugation methods (differential, gradient, equilibrium), electrophoresis methods (SDS, native, isoelectric focussing, immunoelectrophoresis and 2D gel analysis), protein estimation, protein sequencing, protein purification methods (ion-exchange, gel filtration, affinity chromatography), protein characterisation, centrifugation methods (preparative and analytical), UV-visible and fluorescence spectroscopies, mass spectrometry, surface plasmon resonance, radiochemical methods, immunological methods, introduction to X-ray crystallography in protein structure determination, HPLC/GC.

There are two workshops which cover X-ray structural determination of proteins and analysis of data from mass spectrometry.

Learning and teaching

Learning activities and teaching methods (given in hours of study time)

Scheduled Learning and Teaching ActivitiesGuided independent studyPlacement / study abroad
371130

Details of learning activities and teaching methods

CategoryHours of study timeDescription
Scheduled Learning and Teaching16Lectures
Scheduled Learning and Teaching15Laboratory practicals (2 x 6 hours, 1 x 3 hours)
Scheduled Learning and Teaching4Workshops (2 x 2 hours)
Scheduled Learning and Teaching1Practical write-up Q&A session
Scheduled Learning and Teaching1Revision Tutorial
Guided Independent Study1Web-based activities on ELE
Guided Independent Study35Preparation of laboratory and workshop reports
Guided Independent Study77Reading around lecture and practical topics

Assessment

Formative assessment

Form of assessmentSize of the assessment (eg length / duration)ILOs assessedFeedback method
Guided practical write-up session1 x 1 hour; 1 x 2 hours4, 5, 8-12Active discussion
Lecturer and demonstrator feedback during practicals2 x 6 hours, 1 x 3 hours1, 5, 6, 8, 9, 11, 12Oral
Web-based activity on ELE1 x 1 hour4, 11Written

Summative assessment (% of credit)

CourseworkWritten examsPractical exams
40600

Details of summative assessment

Form of assessment% of creditSize of the assessment (eg length / duration)ILOs assessedFeedback method
Examination601 hour1-7, 9-10Written via tutor
Laboratory report251500 words4, 5, 8-12Written
Workshop report15500 words1, 4-6, 9, 10Written

Re-assessment

Details of re-assessment (where required by referral or deferral)

Original form of assessmentForm of re-assessmentILOs re-assessedTimescale for re-assessment
ExaminationExamination1-7, 9-10August Ref/Def
Laboratory reportNot applicableNot applicableNot applicable
Workshop report Not applicableNot applicableNot applicable

Re-assessment notes

Deferral – if you miss an assessment for certificated reasons judged acceptable by the Mitigation Committee, you will normally be either deferred in the assessment or an extension may be granted. The laboratory/practical assessments are not deferrable because of their practical nature. The mark given for a re-assessment taken as a result of deferral will not be capped and will be treated as it would be if it were your first attempt at the assessment.

Referral – if you have failed the module overall (i.e. a final overall module mark of less than 40%) you will be required to sit a further examination. The mark given for a re-assessment taken as a result of referral will count for 100% of the final mark and will be capped at 40%.

Resources

Indicative learning resources - Basic reading

  • Boyer R.F. (2011) Biochemistry Laboratory, Modern Theory and Techniques Pearson, Benjamin/Cummings Publishing Company Inc.

Indicative learning resources - Web based and electronic resources

Module has an active ELE page

Key words search

Macromolecules, proteins, separation techniques, electrophoresis, chromatography, centrifugation, fluorescence spectroscopy, mass spectrometry, surface plasmon resonance, radioactive isotopes, immunology, X-ray crystallography, HPLC, GC, UV-Vis spectroscopy

Credit value15
Module ECTS

7.5

Module pre-requisites

BIO1332 Biochemistry or BIO1341 Biochemistry and Genetics or NSC1003 Foundations in Natural Science

Module co-requisites

None

NQF level (module)

5

Available as distance learning?

No

Origin date

01/02/2013

Last revision date

08/03/2018