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Module - CHEM3012 - Chemical Biology and Enzymes
ProgrammeSoLS - Life Sciences Modules Database (Level 3)
C703 - M.Sci. Hons. Biochemistry (Part 2 - Restricted Group 1)
C700 - B.Sc. Hons. Biochemistry (Part 2 - Restricted Group 2)
Year
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Accrediting Bodies
Module CodeCHEM3012
Credits10
Total Credits:
 
10.00
 
Level:
 
3
 
Target Students:
 
BSc/MSci Chemistry OR Medicinal and Biological Chemistry OR Natural Sciences OR Biochemistry OR Biochemistry and Molecular Medicine OR Biotechnology AND for Level 3 students. Available to JYA/Erasmus students.
 
Summary Of Content:

This module develops an understanding of the nature and structure of enzymes, the characteristics of enzyme catalysed reactions and their inhibition. The mechanisms of action and structures of specific proteases, DNA helicases (PcrA, DnaB and RecBCD), translocases, recombinases and molecular motors, FoF1ATPase and Rho transcriptional terminator are covered. Experimental methodology in biochemistry, molecular biology and chemical biology for cloning genes, expressing proteins in bacteria, strategies for purifying proteins, protein engineering through mutagenesis procedures, N-terminal protein sequencing, protein electrophoresis, determination of protein concentrations, probing biomolecular interactions, assaying the activity of ATPases, protein structure determination(X-ray crystallography and protein NMR) and the use of a range of biophysical techniques. At the end of the module the students should have an understanding of the basic principles of: protein expression, mutagenesis and purification, yeast two and three hybrid technology (Y2H, Y3H), equilibrium sedimentation and velocity sentimentation ultracentrifugation techniques, phage display, surface plasmon resonance (SPR), fluorescence resonance energy transfer (FRET), ATPase assays, microarrays, protein NMR and X-ray crystallography. The students should be able to understand the applications of the above technologies in life science research.

 
 
 
TypeLink
Moodle
 
 

Students should gain a good appreciation of the applications for a range of enzymological, chemical and molecular biological techniques to probe cellular processes and catalysis at the forefront in Chemical Biology research. This module represents a culmination of principles and techniques from a biophysical, molecular, biochemical and genetic perspective.

 
Education Aims:
 
Offering School:
 
Chemistry
 
Convenor:
 
 
 
Name
Prof Panos Soultanas
 
 
 
 
Semester
Autumn UK
 
 
 
Requisites:
 
N/A
 
Additional Requirements:
 
 
 
OperatorCondition
(
Only available for students studying UG Chemistry
OR
Only available for students studying Medicinal and Biological Chemistry
OR
Only available for students studying BSc/MSci Natural Sciences
OR
Only available for students studying Biochemistry
OR
Only available for students studying Biochemistry & Molecular Medicine
OR )
Only available for students studying Biotechnology
AND
Only available for UNUK/Level '03' students
OR
Only available for students studying Biochemistry & Biological Chemistry
 
 
Method and Frequency of Class:
 
 
 
ActivityNumber of WeeksNumber of sessionsDuration of a session
Lecture
10 weeks
1 week
2 hours
Seminar
1 week
1 week
1 hour
 
   
 
Method of Assessment:
 
Assessment TypeWeightRequirements
Exam 1
100.00
3 Hour Exam, Short/Medium Questions 100%. If a further re-assessment is allowed under Undergraduate Course Regulation 19, the form of the re-assessment for this module will be 100% coursework.
 
   
 
Assessment Period:
 
Assessed by end of Autumn Semester
 
     
 
Learning Outcome:
 

At the end of the module, a student should: 

1. Be able to calculate protein concentrations of protein solutions spectrophotometrically. 

2. Understand the principles behind the use of pET vectors for heterologous expression of proteins. 

3. Appreciate the different expression systems available and understand the challenges behind expressing proteins heterologously in Escherichia coli. 

4. Be able to devise basic protein purification protocols based upon the properties of individual proteins. 

5. Understand the basic principles of biophysical techniques used to study molecular interactions. 

6. Differentiate between velocity and equilibrium ultracentrifugation experiments. 

7. Understand the principles behind crystallography and NMR for determination of protein structure. 

8. Understand how the Michaelis-Menten equation is derived and how to produce Lineweaver-Burk plots for reversible inhibitors.

9. Differentiate between competitive and irreversible mechanism based inhibition. 

10. Gain an understanding of the structure and nature of enzymes and how they are classified. 

11. Appreciate the structure/function relationships that underpin enzymatic activities. 

12. Appreciate the molecular mechanisms that motor enzymes like DNA helicases and RecBCD use to convert chemical energy into mechanical motion. 

13. Understand the enzymatic mechanisms used to cleave the peptide bond. 

14. Understand the enzymatic molecular mechanism of ATP synthesis.

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