BS314-6-AU-CO:
Structural and Molecular Enzymology
2018/19
Life Sciences (School of)
Colchester Campus
Autumn
Undergraduate: Level 6
Current
Thursday 04 October 2018
Friday 14 December 2018
15
11 August 2002
Requisites for this module
BS232
(none)
(none)
(none)
(none)
BSC C700 Biochemistry,
BSC C701 Biochemistry (Including Placement Year),
BSC C703 Biochemistry (Including Year Abroad),
BSC CR00 Biochemistry (Including Foundation Year)
You will already have studied simple single site enzymes and have analysed their steady state kinetic behaviour in terms of a model in which an enzyme/substrate complex forms and the substrate is transformed in the active site to yield the product. This model gives directly Michaelis Menten kinetics. This module will begin by considering the steady state kinetic mechanisms of some two-substrate enzymes. We will take a close look at the mechanism of the large class of enzymes termed dehydrogenases and how kinetic measurements and structural investigations enable plausible mechanisms to be deduced.
We also wish to examine more complex systems that comprise many sites which interact through linked protein conformational changes; Allosteric systems. Such systems lead to cooperativity in which initial binding of substrate leads to enhanced (or diminished) binding of further substrate. In this module we will examine such systems and enquire how these effects are produced and what are the biochemical and physiological benefits to the organism of both positive and negative cooperativity. The mechanisms through which allosteric effectors modulate the behaviour of allosteric proteins will be examined and their role in controlling protein action studied. Now that high-resolution structures are available we are able to understand how some of these systems function at the molecular level and a number of examples will be chosen to illustrate the molecular basis of allostery.
Learning Outcomes:
To pass this module students will need to be able to:
1. discuss models (mathematical and structural) of enzyme activity, the mechanisms of allostery and the experimental basis on which the various models of allostery may be distinguished;
2. discuss the mechanism of action of the dehydrogenases and the steady state mechanisms of multi-site enzymes;
3. use key skills, particularly those related to mathematical modelling in the analysis of experimental data.
No information available.
No information available.
Exam assessment: 3 hour paper in Summer Term.
Lectures: 18 x 1 hr including a total of 2hr data analysis and interpretation.
Classes: 2 x 1 hr
Student managed learning: 130 hours/module
Total: 150 hours
This module does not appear to have a published bibliography.
Assessment items, weightings and deadlines
| Coursework / exam |
Description |
Deadline |
Coursework weighting |
| Exam |
Main exam: 180 minutes during Summer (Main Period)
|
Additional coursework information
Summer Exam: wks 33-36
Exam format definitions
- Remote, open book: Your exam will take place remotely via an online learning platform. You may refer to any physical or electronic materials during the exam.
- In-person, open book: Your exam will take place on campus under invigilation. You may refer to any physical materials such as paper study notes or a textbook during the exam. Electronic devices may not be used in the exam.
- In-person, open book (restricted): The exam will take place on campus under invigilation. You may refer only to specific physical materials such as a named textbook during the exam. Permitted materials will be specified by your department. Electronic devices may not be used in the exam.
- In-person, closed book: The exam will take place on campus under invigilation. You may not refer to any physical materials or electronic devices during the exam. There may be times when a paper dictionary,
for example, may be permitted in an otherwise closed book exam. Any exceptions will be specified by your department.
Your department will provide further guidance before your exams.
Overall assessment
Reassessment
Module supervisor and teaching staff
Dr Brandon Reeder, email: reedb@essex.ac.uk.
Dr Brandon Reeder
School Undergraduate Office, email: bsugoffice (Non essex users should add @essex.ac.uk to create the full email address)
Yes
No
No
Dr Clive Butler
The University of Exeter
Associate Professor of Microbial Biochemistry
Available via Moodle
Of 22 hours, 22 (100%) hours available to students:
0 hours not recorded due to service coverage or fault;
0 hours not recorded due to opt-out by lecturer(s).
Disclaimer: The University makes every effort to ensure that this information on its Module Directory is accurate and up-to-date. Exceptionally it can
be necessary to make changes, for example to programmes, modules, facilities or fees. Examples of such reasons might include a change of law or regulatory requirements,
industrial action, lack of demand, departure of key personnel, change in government policy, or withdrawal/reduction of funding. Changes to modules may for example consist
of variations to the content and method of delivery or assessment of modules and other services, to discontinue modules and other services and to merge or combine modules.
The University will endeavour to keep such changes to a minimum, and will also keep students informed appropriately by updating our programme specifications and module directory.
The full Procedures, Rules and Regulations of the University governing how it operates are set out in the Charter, Statutes and Ordinances and in the University Regulations, Policy and Procedures.