recall task Flashcards

1
Q

amino acids are compounds that contain two functional groups (the two that are at either end of the compound). what are they? and what is their chemical formulae?

A

amino group- NH2
carboxylic acid- COOH

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2
Q

what kind of bonds link multiple amino acids?

A

peptide bonds

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3
Q

proteins are polymers of amino acids, of which there are twenty. which functional group differs in each amino acid?

A

R group

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4
Q

what is the primary structure of an amino acid?

A

sequence of amino acids (bonded by peptide bonds)

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5
Q

the secondary structure occurs when what kind of bonds are formed?

A

hydrogen bonds

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6
Q

what are the two types of shapes which can be formed due to these bonds?

A

alpha helix and beta pleated sheets

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7
Q

what is the tertiary structure of a protein?

A

3D structure

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8
Q

name the three additional bonds formed in the tertiary structure

A

hydrogen
ionic
disulfide

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9
Q

what is the quaternary structure of a protein?

A

more than 1 polypeptide chain bonded together

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10
Q

give an example of a globular protein and its function

A

haemoglobin-transport
pepsin-enzymes
insulin-hormone

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11
Q

give an example of a fibrous protein and its function

A

collagen-structural support
keratin-protection/waterproofing

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12
Q

what is an enzyme?

A

protein molecule-biological catalyst

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13
Q

what part of the enzyme is unique and complementary to the substrate?

A

active site

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14
Q

explain, simply, what the collision theory is with respect to enzymes and substrates

A

particles must collide, (enzymes and substrates much physically collide with each other) in the correct orientation (the substrate must collide with the enzymes active site in the right position), and with sufficient energy (the collision must have enough energy to overcome the activation energy barrier and allow the reaction to proceed).

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15
Q

name two things that can impact the frequency of collisions and therefore rate of reaction

A

changing temp, concentration (of substrate or enzyme), and surface area of substrate

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16
Q

what is the intermediate step (thing that is formed) when an enzyme reacts with the substrate?

A

enzyme substrate complex

17
Q

what’s the difference between the lock and key and the induced fit models?

A

lock and key- active site shape is unique
induced fit- active site changes to better fit substrate

18
Q

what is activation energy?

A

minimum amount of energy needed for a reaction to take place

19
Q

how does temperature effect the rate of reaction?

A

increase temperature = increased rate of reaction

20
Q

how does concentration of substrate affect the rate of reaction?

A

increased concentration = increased rate of reaction

21
Q

how does the surface area affect the rate of reaction?

A

increased surface area = increased rate of reaction

22
Q

what is it called when the shape of the active site changed, preventing binding of the substrate to the enzyme?

A

denaturing

23
Q

what is the term used to temperature and pH, where the rate of reaction is the greatest?

24
Q

what is a competitive inhibitor and is the binding of this inhibitor reversible or non-reversible?

A

binds to active site and “competes” with substrate for binding - reversible

25
what is a non-competitive inhibitor and is the binding of this inhibitor reversible or non-reversible?
binds to another site on the enzyme that isn’t the active site - non-reversible