BS314-6-SP-CO:
Structural and Molecular Enzymology
2024/25
Life Sciences (School of)
Colchester Campus
Spring
Undergraduate: Level 6
Current
Monday 13 January 2025
Friday 21 March 2025
15
14 February 2024
Requisites for this module
(none)
(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),
MSCIC098 Biochemistry and Biotechnology (Including Year Abroad),
MSCIC099 Biochemistry and Biotechnology (Including Placement Year),
MSCICZ99 Biochemistry and Biotechnology
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.
This module will also examine more complex systems that comprise many sites which interact through linked protein conformational changes; Allosteric systems.
The aim of this module is:
- To build upon knowledge gained in previous years.
By the end of this module, students will be expected to be able to:
- 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.
- Discuss the mechanism of action of the dehydrogenases and the steady state mechanisms of multi-site enzymes.
- Use key skills, particularly those related to mathematical modelling in the analysis of experimental data.
Students 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.
Allosteric 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.
This module will be delivered via:
- Eighteen 1-hour lectures including a total of 2hr data analysis and interpretation.
- Two 1-hour classes.
- Student managed learning.
This module does not appear to have a published bibliography for this year.
Assessment items, weightings and deadlines
| Coursework / exam |
Description |
Deadline |
Coursework weighting |
| Exam |
Main exam: In-Person, Open Book (Restricted), 180 minutes during Summer (Main Period)
|
| Exam |
Reassessment Main exam: In-Person, Open Book (Restricted), 180 minutes during September (Reassessment Period)
|
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
Prof Jonathan Worrall, email: jworrall@essex.ac.uk.
Prof Jonathan Worrall
School Undergraduate Office, email: bsugoffice (Non essex users should add @essex.ac.uk to create the full email address)
Yes
No
No
Prof Richard Bowater
University of East Anglia
Professor of Biochemistry and Molecular Biology Education
Available via Moodle
Of 9 hours, 9 (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), module, or event type.
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