IB Biology Standard 2.4 Proteins Lecture

2. Molecular Biology (Core) – 2.4 Proteins Name:
Understandings, Applications and Skills (This is what you maybe assessed on)
Statement Guidance
2.4.U1 Amino acids are linked together by condensation to form
http://bioknowledgy.weebly.com/ (Chris Paine)
polypeptides.
2.4.U2 There are 20 different amino acids in polypeptides
synthesized on ribosomes.
Students should know that most organisms
use the same 20 amino acids in the same
genetic code although there are some
exceptions. Specific examples could be
used for illustration.
2.4.U3 Amino acids can be linked together in any sequence giving
a huge range of possible polypeptides.
2.4.U4 The amino acid sequence of polypeptides is coded for by
genes.
2.4.U5 A protein may consist of a single polypeptide or more than
one polypeptide linked together.
2.4.U6 The amino acid sequence determines the three-dimensional
conformation of a protein.
2.4.U7 Living organisms synthesize many different proteins with a
wide range of functions.
2.4.U8 Every individual has a unique proteome.
2.4.A1 Rubisco, insulin, immunoglobulins, rhodopsin, collagen
and spider silk as examples of the range of protein
functions.
The detailed structure of the six proteins
selected to illustrate the functions of
proteins is not needed.
2.4.A2 Denaturation of proteins by heat or by deviation of pH from
the optimum.
Egg white or albumin solutions can be used
in denaturation experiments.
2.4.S1 Drawing molecular diagrams to show the formation of a
peptide bond.
Recommended resources:
http://bioknowledgy.weebly.com/24-proteins.html
Allott, Andrew. Biology: Course Companion. S.l.: Oxford UP, 2014. Print.

2.4.U1 Amino acids are linked together by condensation to form polypeptides. AND
2.4.S1 Drawing molecular diagrams to show the formation of a peptide bond.
1. Condensation of amino acids is a polymerisation reaction. A chain of amino acids joined together is
called a polypeptide. These building reactions are part of the anabolic metabolism.
a. What structure mediates and controls the formation of polypeptides?
b. Apart from the above structure what else is needed for the reaction to occur?
c. Draw and annotate a structural diagram below to outline how two generalised amino acids (i.e. use
the R-group nomenclature) into a dipeptide through condensation, producing a peptide bond.
2.4.U2 There are 20 different amino acids in polypeptides synthesized on ribosomes.
2. How many different amino acids do we know of?
22
3. How many of these amino acids are synthesised by ribosomes?
20

4. List three examples of amino acids synthesised by ribosomes.



5. Extension: Outline the process by which the remaining amino acids are created.
2.4.U3 Amino acids can be linked together in any sequence giving a huge range of possible polypeptides.
6. State the three key ideas that explain the huge range of possible polypeptides:



7. If a polypeptide contains just 5 amino acids calculate the how many different polypeptides can be
created.
8. State both the name of the longest polypeptide known and approximately how many amino acids it
contains.
2.4.U4 The amino acid sequence of polypeptides is coded for by genes.
9. Outline the central dogma of genetics.

2.4.U6 The amino acid sequence determines the three-dimensional conformation of a protein.
2.4.U5 A protein may consist of a single polypeptide or more than one polypeptide linked together.
10. The R-groups of an amino acid are classified as having one of a number of different properties. List the
properties can they possess.




11. Extension: complete the table to outline the four different levels of protein structure. (n.b. although you
don’t need to be able to outline the different levels of structure knowing of them helps to understand the
different functions proteins have and why)
Notes Fibrous or Globular
Primary
(polypeptide)
• The order / sequence of the amino acids of which the
protein is composed
• Formed by covalent peptide bonds between adjacent amino
acids
• Controls all subsequent levels of structure
Neither (– will fold to
become one of the
subsequent levels of
structure)
Secondary
Tertiary
Quaternary

12. Distinguish between globular and fibrous proteins
Fibrous Globular
Location of
R groups
Shape
Function
Solubility
Amino acid
sequence
Stability
Examples

2.4.U7 Living organisms synthesize many different proteins with a wide range of functions.
13. Complete the table to describe each of different functions that proteins have in and outside of cells.
Function Description Key examples
Rubisco
Muscle contraction
Tubulin is the subunit of microtubules that give animals cells their
shape and pull on chromosomes during mitosis.
collagen
Blood clotting
Proteins in blood help transport oxygen, carbon dioxide, iron and
lipids.
Cell adhesion
Membrane transport
Insulin
Receptors
rhodopsin
Packing of DNA
This is the most diverse group of proteins, as cells can make huge
numbers of different antibodies.
immunoglobulins

2.4.A1 Rubisco, insulin, immunoglobulins, rhodopsin, collagen and spider silk as examples of the range of
protein functions.
14. Take notes to outline each of the key examples of protein function.
Rubisco:
insulin:
immunoglobulins:
rhodopsin:

collagen:
spider silk:
2.4.U8 Every individual has a unique proteome.
15. The proteome is unque to every individual.
a. Define the term genome.
b. Define the term proteome.
c. Aside from the genome what affects the proteome?

d. Explain why the proteome is larger and more varied that the genome.
2.4.A2 Denaturation of proteins by heat or by deviation of pH from the optimum.
16. Describe the term denaturation. Refer to the structure of the protein in your answer.
17. What factors can commonly cause denaturation and how?
Citations:
Allott, Andrew. Biology: Course Companion. S.l.: Oxford UP, 2014. Print.

IB Biology Standard 2.4 Proteins Lecture

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IB Biology Standard 2.4 Proteins Lecture