Module Catalogues, Xi'an Jiaotong-Liverpool University   
Module Code: BIO207
Module Title: Proteins in Action
Module Level: Level 2
Module Credits: 2.50
Academic Year: 2020/21
Semester: SEM1
Originating Department: Biological Sciences
Pre-requisites: N/A
This module is designed to illustrate how proteins function at the molecular level, with respect to transport, localization, structure and interacting molecules. The modes of action of example proteins and the other molecules with which they interact are explained in terms of the chemistry of the reactants involved. In addition, the examples given in the module will be used to introduce or re-introduce aspects of physical biochemistry such as pKa, reduction potential, reaction kinetics and proton motive force which can be unpalatable if taught in isolation. The regulation and evolution of proteins and their functions will also be discussed.
Learning outcomes 
At the end of this module students will acquire knowledge and critical understanding of the principles of:

A. Nomenclature, structure and function of example enzymes

B. The function and mechanism of action of coenzymes

C. The structural and functional interactions between proteins and membranes

D. The various means of regulating protein function.

E. The principal modes of protein evolution and function

F. Protein secretion and protein transport processes

Method of teaching and learning 
Module content will be delivered primarily via standard lectures, the slides of which will be made available. Students will also be guided to sections of specific textbooks or specific reviews or source literature.

During the module, revision lectures/exercises will allow the students to self-assess their understanding.

The following topics will be addressed (glossary).

Enzyme nomenclature and classification (examples of the six E.C. classes).

Stereochemistry and conformation (revision of chirality, diastereoisomers, nomenclature (e.g. dl, DL, RS), stereospecificity of enzymes).

Enzyme kinetics and inhibition (rates of chemical reactions, review of rate constants, first and second order reactions, equilibria, Kd, ES complex, saturation, enzyme kinetics, the Michaelis-Menten equation, Km, Vmax, kcat, enzyme inhibition, competitive, uncompetitive, effect on Km, Vmax, coenzymes, vitamins as precursors, transamination, racemization, decarboxylation, elimination reactions).

Proteases (serine proteases, catalytic triad, site-directed mutagenesis, specificity pocket).

Protein regulation (regulation by covalent modification: splicing of propeptides, phosphorylation, acetylation, regulation without covalent modification: allosteric control by effectors; regulation by change in quaternary structure, binding of inhibitors to catalytic site, regulation by environment, e.g. pH, glycogenolysis).

Protein evolution (the connection to bioinformatics, evolution of protein function by mutation and by domain duplication / shuffling, homology, orthology, paralogy, structural and/or functional conservation while sequence changes, moonlighting proteins, convergent evolution, molecular mimicry).

Membrane proteins (various structure and functions of membrane proteins, examples of how proteins work in combination with membranes, usage of various means [light, electron transfer] to generate a proton motive force, membrane-based molecular motors, cytochromes in mitochondrial oxidative phosphorylation, electron transfer, domain changes and proton pumping, ATP synthase, structure and the mechanism through which it catalyses the phosphorylation of ADP).

Delivery Hours  
Lectures Seminars Tutorials Lab/Prcaticals Fieldwork / Placement Other(Private study) Total
Hours/Semester 26    2      47  75 


Sequence Method % of Final Mark
1 Final Exam 85.00
2 Continuous Assessment 15.00

Module Catalogue generated from SITS CUT-OFF: 6/7/2020 4:37:39 AM