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sl bio proteins and enzymes Flashcards

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Biology 101 flashcards
1
Q

what type of anabolism is used to make peptide bonds

A

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

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2
Q

how many amino acids?

A

21

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3
Q

how many essential amino acids?

A

9

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4
Q

what is the man made amino acid called?

A

hydroxyproline

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5
Q

dna to RNA is the?

A

transcription

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6
Q

RNA to polypeptide is the?

A

translation

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7
Q

genes are simply codes for making what?

A

polypeptides

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8
Q

polypeptides is produced where in the cell?

A

in the cytoplasm by ribosomes

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9
Q

what is mRNA?

A

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

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10
Q

what tells ribosomes what amino acids to use?

A

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

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11
Q

polypeptides is joined by what?

A

peptide bonds

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12
Q

how is peptide bonds made?

A

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

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13
Q

what are the four protein structures?

A

primary, secondary, tertiary, and Quaternary

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14
Q

what are the attributes of primary structure?

A

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

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15
Q

what are the attributes of secondary structure?

A

-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

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16
Q

what are the attributes of tertiary structure?

A

-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

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17
Q

what are the attributes of Quaternary structure?

A

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

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18
Q

fibrous protein shape:

A

long and narrow

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19
Q

globular protein shape:

A

rounded/spherical

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20
Q

fibrous protein role:

A

structural

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21
Q

globular protein role:

A

functional

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22
Q

fibrous protein solubility:

A

insoluble

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23
Q

fibrous protein stability?

A

less sensitive to heat, ph, etc.

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24
Q

globular protein solubility?

A

soluble

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25
Q

globular protein stability?

A

more sensitive to heat, ph, etc.

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26
Q

fibrous protein examples:

A

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

27
Q

globular protein example:

A

-catalase
-hemoglobin
-insulin
immunoglobulin

28
Q

catalysis function:

A

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

29
Q

muscle contraction function:

A

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

30
Q

cytoskeletons:

A

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

31
Q

tensile strengthening

A

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

32
Q

blood clotting

A

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

33
Q

transport nutrients and gas

A

proteins help transport oxygen, carbon dioxide, iron and lipids

34
Q

cell adhesion

A

membrane causes proteins to stick to each other within tissues

35
Q

membrane transport

A

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

36
Q

hormones

A

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

37
Q

receptors

A

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

38
Q

Packing of DNA

A

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

39
Q

Immunity

A

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

40
Q

rubisco is an example of what function?

A

catalysis

41
Q

collagen is an example of function?

A

tensile strengthening

42
Q

insulin is an example of what function?

A

hormones

43
Q

rhodopsin is an example of what function?

A

receptors

44
Q

immunoglobulin is an example of what function?

A

immunity

45
Q

what is an enzyme?

A

a globular protein which acts as a catalyst for biochemical reactions

46
Q

what is a substrate?

A

a reactant in a biochemical reaction

47
Q

what is the active site?

A

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

48
Q

what is induced fit?

A

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

49
Q

what is denaturation?

A

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

50
Q

what is optimal temperature?

A

when the enzyme activity is at its peak

51
Q

at what pH level do enzymes like?

A

7 or 7.2

52
Q

what is optimum concentration?

A

when all active sites are working at maximum efficiency

53
Q

what does detergent do?

A

contain proteases and
lipases to help breakdown protein and fat stains

54
Q

biofuels:

A

enzymes are used to break down grains into biofuels

55
Q

textiles:

A

polish clothing

56
Q

brewing:

A

clarification of the beer

57
Q

medicine and biotechnology:

A

diagnostic tests, cutting dna, contact lens cleaners, etc

58
Q

food:

A

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

59
Q

concentration:

A

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

60
Q

recycled:

A

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

61
Q

seperation

A

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

62
Q

stability

A

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

63
Q

what is lactose intolerance?

A

when the embody doesn’t produce enough lactase

64
Q

how can milk be lactose free?

A

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.

bio (3 decks)

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