sl bio proteins and enzymes

Question 1

what type of anabolism is used to make peptide bonds

Answer 1

condensation; a ribosome condenses two amino acids into a dipeptide forming a peptide bond

Question 2

how many amino acids?

Answer 2

21

Question 3

how many essential amino acids?

Answer 3

9

Question 4

what is the man made amino acid called?

Answer 4

hydroxyproline

Question 5

dna to RNA is the?

Answer 5

transcription

Question 6

RNA to polypeptide is the?

Answer 6

translation

Question 7

genes are simply codes for making what?

Answer 7

polypeptides

Question 8

polypeptides is produced where in the cell?

Answer 8

in the cytoplasm by ribosomes

Question 9

what is mRNA?

Answer 9

mRNA is the messages RNA from the nucleus to ribosomes to carry instructions on how to put the polypeptide together

Question 10

what tells ribosomes what amino acids to use?

Answer 10

the genetic code, its the sequence of bases on the mRNA

Question 11

polypeptides is joined by what?

Answer 11

peptide bonds

Question 12

how is peptide bonds made?

Answer 12

by condensation of anabolism which removes the water and makes it a product

Question 13

what are the four protein structures?

Answer 13

primary, secondary, tertiary, and Quaternary

Question 14

what are the attributes of primary structure?

Answer 14

-forms covalent peptide bonds between adjacent amino acids
-controls all sub sequential levels of structure

Question 15

what are the attributes of secondary structure?

Answer 15

-chains of amino acids fold amongst themselves
-held together by hydrogen bonds
between (non-adjacent) amine
(N-H) and carboxylic (C-O) groups
-H-bonds provide a level of structural stability
-fibrous proteins

Question 16

what are the attributes of tertiary structure?

Answer 16

-The polypeptide folds and
coils to form a complex
3D shape
-Caused by interactions
between R groups (H-
bonds, disulphide
bridges, ionic bonds and
hydrophilic / hydrophobic
interactions)
- Tertiary structure may be
important for the
function
-globular protein

Question 17

what are the attributes of Quaternary structure?

Answer 17

-The interaction
between multiple
polypeptides or
prosthetic groups
-A prosthetic group
is an inorganic
compound
involved in a
protein
-fibrous or globular protein

Question 18

fibrous protein shape:

Answer 18

long and narrow

Question 19

globular protein shape:

Answer 19

rounded/spherical

Question 20

fibrous protein role:

Answer 20

structural

Question 21

globular protein role:

Answer 21

functional

Question 22

fibrous protein solubility:

Answer 22

insoluble

Question 23

fibrous protein stability?

Answer 23

less sensitive to heat, ph, etc.

Question 24

globular protein solubility?

Answer 24

soluble

Question 25

globular protein stability?

Answer 25

more sensitive to heat, ph, etc.

Question 26

fibrous protein examples:

Answer 26

-collagen -myosin -fibrin -actin -keratin -elastin

Question 27

globular protein example:

Answer 27

-catalase -hemoglobin -insulin immunoglobulin

Question 28

catalysis function:

Answer 28

There are thousands of different enzymes to catalyse specific chemical reactions within the cell or outside it.

Question 29

muscle contraction function:

Answer 29

actin and mysosin together cause the muscles to contractions used in locomotion and transport around the body

Question 30

cytoskeletons:

Answer 30

tubulin is the subunit of microtubules that give animal cells their shapes and pull on chromosomes during mitosis

Question 31

tensile strengthening

Answer 31

fibrous proteins give tensile strength in skin, tendons ligaments, and blood vessels

Question 32

blood clotting

Answer 32

plasma proteins act as clotting factors that cause blood to turn from liquid to gel in wounds

Question 33

transport nutrients and gas

Answer 33

proteins help transport oxygen, carbon dioxide, iron and lipids

Question 34

cell adhesion

Answer 34

membrane causes proteins to stick to each other within tissues

Question 35

membrane transport

Answer 35

Membrane proteins are used for facilitated diffusion and active transport, and also for electron transport during cell respiration and photosynthesis

Question 36

hormones

Answer 36

Some such as insulin, FSH and LH are proteins, but hormones are chemically very diverse.

Question 37

receptors

Answer 37

Binding sites in membranes and cytoplasm for hormones, neurotransmitters, tastes and smells, and also receptors for light in the eye and in plants

Question 38

Packing of DNA

Answer 38

Histones are associated with DNA in eukaryotes and help chromosomes to condense during mitosis.

Question 39

Immunity

Answer 39

This is the most diverse group of proteins, as cells can make huge numbers of different antibodies.

Question 40

rubisco is an example of what function?

Answer 40

catalysis

Question 41

collagen is an example of function?

Answer 41

tensile strengthening

Question 42

insulin is an example of what function?

Answer 42

hormones

Question 43

rhodopsin is an example of what function?

Answer 43

receptors

Question 44

immunoglobulin is an example of what function?

Answer 44

immunity

Question 45

what is an enzyme?

Answer 45

a globular protein which acts as a catalyst for biochemical reactions

Question 46

what is a substrate?

Answer 46

a reactant in a biochemical reaction

Question 47

what is the active site?

Answer 47

region on the surface of an enzyme to which substrates bind and catalyses to a reaction

Question 48

what is induced fit?

Answer 48

a confrontational change in the active site to fit the substrate yet this stresses the substrate and causes it to reduce activation energy

Question 49

what is denaturation?

Answer 49

when the shape of the enzyme is irreversibly changed due affected levels of heat, substrate concentration, or pH which causes it to be ruined

Question 50

what is optimal temperature?

Answer 50

when the enzyme activity is at its peak

Question 51

at what pH level do enzymes like?

Answer 51

7 or 7.2

Question 52

what is optimum concentration?

Answer 52

when all active sites are working at maximum efficiency

Question 53

what does detergent do?

Answer 53

contain proteases and lipases to help breakdown protein and fat stains

Question 54

biofuels:

Answer 54

enzymes are used to break down grains into biofuels

Question 55

textiles:

Answer 55

polish clothing

Question 56

brewing:

Answer 56

clarification of the beer

Question 57

medicine and biotechnology:

Answer 57

diagnostic tests, cutting dna, contact lens cleaners, etc

Question 58

food:

Answer 58

pectin for juice, isomerase for fructose, rennin for cheese, etc

Question 59

concentration:

Answer 59

of substrate can be increased as the enzyme is not dissolved – this increases the rate of reaction

Question 60

recycled:

Answer 60

enzymes can be used many times, immobilized enzymes are easy to separate from the reaction mixture, resulting in a cost saving.

Question 61

seperation

Answer 61

of the products is straight forward (this also means that the the reaction can stopped at the correct time).

Question 62

stability

Answer 62

of the enzyme to changes in temperature and pH is increased reducing the rate of degradation, again resulting in a cost saving.

Question 63

what is lactose intolerance?

Answer 63

when the embody doesn't produce enough lactase

Question 64

how can milk be lactose free?

Answer 64

milk with lactose is passed through lactose beads extracted from yeast or bacteria multiple times until the lactose is immobilized and turns into galactose and glucose again.