o Describe the macromolecular structure of proteins in terms of primary, secondary,

tertiary and quaternary structure

o Describe the common structural motifs adopted by folded proteins and discuss how
their three dimensional shapes are stabilised by non-covalent forces
o Explain, in outline, the methodology, advantages and limitations of methods used to
determine protein structure
o Describe the principles by which enzymes catalyse biochemical reactions and
describe in detail the reaction mechanism of named enzymes
o Explain how changes in environment can affect protein activity and describe the effect
of changes in substrate concentration, pH, temperature and the binding of nonsubstrate ligands on protein and enzyme structure:function
o Analyse and interpret experimental data from the results of a series of experiments
aiming to characterize the kinetics of an enzyme, and communicate these effectively in
written form in the style of a full scientific laboratory report
o Record accurately and appropriately the purpose, methodology, results and data
analysis relating to experimental investigations in a laboratory notebook
End of Module
Exam

65%

Split into three sections

(Section A, worth one
third of the exam mark
is a series of short
answer
questions
covering the range of
topics from the lecture
course. Sections B and
C are a choice of essay
out of two; section B
questions
deal
with
protein structure and
section C essays with
protein
structure:function.
Students should answer
one question from each
section,
each essay
contributes one third of
the exam mark).

Date
TBA
from
the
examinations
office
(Autumn
semester
examination
period,
Jan
2015)

Generic feedback
will be available
on the KLE from
mid-February

12