AMG How to Study Biochemistry
How to Study Biochemistry
Hello, dear friend, you can consult us at any time if you have any questions, add WeChat: THEend8_
AMG
How to Study Biochemistry
1. The Map Analogy: Learning
biochemistry is like learning to navigate
using a map (can you identify
similarities?)
2. Start with the Essentials: divide
learning content into blocks (topics)
and familiarise yourself with answers to
basic questions
3. Draw it: drawing helps you remember;
creativity powers science
4. Re-visit, revise, repeat, connect,
build: repetition helps you consolidate
the basics so that broader connections
can be made
How do you learn biochemistry?
B O
I
H
C
Millie
• You don’t need to memorise all the
street names in order to read and
understand a map
• First focus on how to identify and
understand the key features of
biochemical pathways so you can apply
the same approach to new pathways
2. Start with the Essentials:
How do you learn biochemistry?
• Is it an anabolic or catabolic pathway?
• What is its function?
• Where in the cell does it occur?
• In what tissues does it occur?
• What are the key control mechanisms?
• Are there typical starting/endpoint
molecules?
• Are energy molecules (ATP/GTP)
produced or consumed? How many?
• Are reduced cofactors (NADH/FADH)
produced or consumed? How many?
Where?
3. Draw it
How do you learn biochemistry?
• Draw: lecture summaries, biochemical pathway summaries,
physical locations of pathways, concept diagrams (e.g.
mechanism of enzyme action, chemiosmotic theory etc.)
• Make your drawings visible/accessible: stick them up
around your room, make a scrap-book, or wall-paper your
phone/computer!
• Extend your creativity: if you are on a roll, try
communicating science using other approaches – e.g.
cartoons, aesthetic imagery, videos, apps/games
Anne’s Mito Membranes
How do you learn biochemistry?
• This metabolic
summary schematic is
a great example of a
visual means for linking
concepts in BIOC2101
• You might like to use
this as a basis for your
own learning maps or
create your own
3. Draw it
4. Re-visit, revise,
repeat, connect,
build
How do you learn biochemistry?
• Biochemistry doesn’t usually just
‘sink in’ overnight
• Regular revision in small doses
helps you remember the basics
• This helps you to see patterns
and trends, thus helping you to
make higher-level connections
and inferences
AMG
Exam Techniques
Tips for Writing Good Essay and
Short Response Answers
AMG
General Biochemistry Study Tips
The following study suggestion was made at the beginning of the course. It addresses
individual biochemical pathways. While the lectures on individual pathways are not directly
being examined in the final exam, this has been included here as a reminder, as it may still
help support your studies of the integration lectures for the final exam.
Study Suggestion
For each biochemical pathway that you have learned about, try to answer the following 10
questions (based on a human system):
1. What is the name of the pathway? Are there any alternative names?
2. Does it have a specific location in the cell? Where?
3. Does it have one or more tissue-specific locations in the body?
4. What is/are the primary function/s of the pathway?
5. Is there a main starting molecule of the pathway? What is it?
6. Is there a main product of the pathway? What is it?
7. Are there one or more key regulatory (control) enzymes in the pathway?
What are they?
8. Is the pathway regulated allosterically and/or hormonally?
9. Under what conditions is the pathway more likely to be activated?
10. Under what conditions is the pathway more likely to be inactivated?
AMG
What do you think makes a good
short essay answer good???
AMG
A GOOD short essay answer should:
• ANSWER THE QUESTION!!!
• Be clear and concise.
• Have a logical flow of ideas, information or
arguments.
• Be legible. (Be legible).
• Demonstrate a satisfactory to comprehensive
understanding of the relevant theoretical or
conceptual material.
• Use appropriate language and terminology.
DO YOU AGREE???
AMG
The following activity provides a sample
extended response question (not relating to
your final exam) with marking guidelines
that were used to mark it and sample
student responses with associated marks.
This is a guide only. The Question shown
would typically be marked out of 10.
AMG
A Biochemistry Short Essay Question
from a Previous Year:
List and describe the four major levels of protein
structure. In your answer, include information about
the types of bonds and/or interactions that occur at
each level. (Include diagrams where appropriate)
AMG
Marking Guidelines
1. List and describe the four major levels of protein structure. In your
answer, include information about the types of bonds and/or interactions
that occur at each level. (Include diagrams where appropriate).
2-5 marks were allocated to each level of protein structure depending
on the level of detail taught and expected in responses. These marks
were then divided into 0.5 or 1 mark for each correct point or statement
made for each level. Note that a student cannot gain more than the
maximum number of marks allocated (below) for each level of structure.
Information can be presented in a clear diagram and/or in the text. Each
‘informative’ figure gets 0.5 marks.
An example of the marks allocated for potential responses is as follows
(please note that either 0.5 or 1 mark are awarded in each case and
weighted according to the relevance or importance of each point):
AMG
Marking Guidelines
Primary Structure (worth 4 marks in total):
•Primary structure of a protein is its unique sequence of amino acids (1
mark) linked together by peptide bonds (1 mark), N-terminal to C-terminal
(0.5 marks). (Full marks for this section are not given if peptide bonds are
not mentioned).
•Like the order of letters in a very long word (0.5 marks)
•The sequence is determined by inherited genetic information (1 mark).
•Diagram of chain of letters (0.5 marks) and/or peptide bonds (0.5 marks).
Secondary Structure (worth 5 marks in total):
• Refers to the conformation adopted by local regions of the polypeptide
chain (1 mark).
•Secondary structures include the alpha helix (0.5 marks) and beta
strands/sheets (0.5 marks).
•These secondary structures depend on hydrogen bonding (0.5 marks)
between backbones (0.5 marks)
•Loops and turns are other secondary structures (0.5 marks).
•0.5 marks can be given for additional details or figures of the structure for
each of the alpha helix, beta-sheet and turns/loops.
AMG
Marking Guidelines
Tertiary Structure (worth 5 marks in total):
•Consists of irregular contortions resulting from interactions between the side chains
of the various amino acids (1 mark) (do not award full marks for this section if “side-
chain interactions” are not referred to at some stage).
•A polypeptide chain will fold so that its hydrophobic side chains are buried and its
polar/charged side chains are on the surface (1 mark).
•Weak interactions contributing to the tertiary structure include hydrophobic
interactions, hydrogen bonds and ionic/electrostatic bonds (0.5 marks each).
•Although these bonds are weak, their cumulative effect helps give the protein a
specific shape (0.5 marks).
•Stronger covalent disulfide bonds/bridges also exist (0.5 marks).
•Up to 1 mark for good figure illustrating bonds.
•1 mark for protein folding as a reduction in free energy.
Quaternary Structure (worth 2 marks in total):
•Proteins consisting of more than one polypeptide chain display quaternary structure
(1 mark).
•Quaternary structure can be as simple as two identical subunits or as complex as
dozens of different subunits (0.5 marks).
•In most cases, the subunits are held together by non-covalent bonds (0.5 marks)
but also covalent disulphide bonds (0.5 marks).
AMG
Now let’s look at some of the actual
STUDENT answers to this essay question!
There are 5 different student responses shown.
You can observe the merits and/or weaknesses of each
response and then look at the following slide where the
mark allocations and final mark are shown for that response.