L2

Question 1

The Functions of DNA

Answer 1

1. To store information
2. To replicate faithfully
3. Allow for a slow changes over time (mutations

Question 2

What gives protein diversity

Answer 2

exon splicing
post-translational modifications

Question 3

Types of post-translational modifications

Answer 3

• Proteolytic cleavage
• Addition of chemical groups

Question 4

Examples of chemical groups

Answer 4

phosphate
acetyl
methyl
glycans
GPI anchors
hydroxyl
sulfate
ubiquitin
nitro

Question 5

What does addition of a phosphate group do

Answer 5

for activation and inactivation of enzymes

Question 6

what does addition of an acetyl group do

Answer 6

for protein stability and is used in histones

Question 7

what is methylation used for

Answer 7

regulation of gene expression

Question 8

what is glycosylation used for

Answer 8

cell-cell recognition and signalling

Question 9

what is the GPI anchor used for

Answer 9

membrane tethering

Question 10

what is hydroxyproline used for

Answer 10

• protein stability, ligand interactions

Question 11

what is sulfation used for

Answer 11

protein-protein and ligand interactions

Question 12

what is disulfide bond formation used for

Answer 12

protein stability

Question 13

what is deamidation used for

Answer 13

protein-protein and ligand interaction

Question 14

what is ubiquitination used for

Answer 14

destruction signal

Question 15

what is nitration of tyrosine used for

Answer 15

inflammation

Question 16

Proteomics is used to investigate?

Answer 16

WRHTTH

Question 17

W

Answer 17

when and where proteins are expressed

Question 18

R

Answer 18

rates of protein production, degradation, and steady-state abundance

Question 19

H

Answer 19

how proteins are modified

Question 20

T

Answer 20

the movement of proteins between subcellular compartments

Question 21

T

Answer 21

the involvement of proteins in metabolic pathways

Question 22

H

Answer 22

how proteins interact with one another

Question 23

Plasma components

Answer 23

• plasma proteins
• tissue proteins
• immunoglubulins

Question 24

How many forms of plasma proteins are there and how do they arise?

Answer 24

40,000 forms and they arise through genetic variants (500 gene variants), alternative splicing (twice as many splice variants), glycosylation (20 different glycoforms per variant), and cleavage

Question 25

How many forms of tissue proteins are there and how do they arise

Answer 25

500,000 forms and are derived from around 23,000 genes, with each gene having an average of 5 splice variants and undergoing 5 post-translational modifications (PTMs).

Question 26

How many forms of immunoglobulin are there?

Answer 26

10 million different clonal forms of immunoglobulins

Question 27

Protein structure can be divided into

Answer 27

Primary (amino acid sequence)
- Secondary (local folding structure)
- Tertiary (overall fold of amino acid chain)
- Quaternary (subunits composing functional protein)

Question 28

what determines the amino acid property

Answer 28

different side chains

Question 29

How is the alpha helix of a protein structure made

Answer 29

the carbonyl
(C=O) of one amino acid is
hydrogen bonded to the
amino H (N-H) of an amino
acid that is four down the
chain.

Question 30

how is the beta sheet of a protein structure made-

Answer 30

In a β pleated sheet, two
or more segments of a
polypeptide chain line up
next to each other, forming
a sheet-like structure held
together by hydrogen
bonds. The strands of a β pleated
sheet may be parallel,
or antiparallel

Question 31

CTFR protein function

Answer 31

a channel for the movement of chloride ions in and
out of cells, which is important for the salt and water balance on epithelial surfaces,
such as in the lungs or pancreas. Changes in the CFTR gene can affect the
structure of the CFTR protein.