B1.2 Proteins Flashcards

1
Q

what monomers make up proteins

A

amino acids

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2
Q

what determines the shape and function of the protein

A

the sequence, type and number of amino acids present

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3
Q

how many naturally occurring amino acids there

A

20

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4
Q

amino acid + amino acid

A

dipeptide

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5
Q

how many essential amino acids are there

A

9

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6
Q

what are essential amino acids

A

amino acids that can’t be synthesised

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7
Q

what does the genetic code (DNA base sequence) code for

A

the number and order of amino acids in a polypeptide

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8
Q

for a chain of 50 amino acids, how many possible combinations would there be

A

20^50

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9
Q

some roles of proteins

A

catalysis by enzymes
blood clotting - interact w oxygen to form scab
strengthen fibres in skin (collagen, keratin)
immune system antibodies
hormones

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10
Q

how does heat denaturation affect protein structure

A

heat causes vibrations within protein molecules, breaking intramolecular bonds so conformation changes
irreversible

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11
Q

how does pH affect protein structure

A

pH change causes intramolecular bonds to break within the protein molecule

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12
Q

why is there a lot of chemical diversity between the amino acids

A

the r groups vary a lot between the 20 amino acids

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13
Q

role of r groups

A

determine properties of amino acids- acidic/basic, polar/non polar etc

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14
Q

___________ R groups are polar and can be either acidic or basic

A

Hydrophillic

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15
Q

what are proteins

A

relatively large complex molecules that contain one or more chains of amino acids known as polypeptides

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16
Q

what is primary structure

A

the sequence of amino acids in a polypeptide chain

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17
Q

what is secondary structure

A

the formation of secondary structures - alpha helices and beta pleated sheets

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18
Q

why do these secondary structures form

A

as a result of hydrogen bonding between different amino acids in the chain

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19
Q

what happens in the tertiary structure

A

how the secondary structures fold to form a 3d structure

20
Q

what does the folding in the tertiary structure result from

A

the interactions between the r groups of the amino acids and the environment

20
Q

what types of bonding are there in the tertiary structure

A

peptide bonds
hydrogen bonds( r groups +amino+carboxyl groups)
disulfide
ionic
hydrophobic interactions

21
Q

are the amino acids in protein polar or non polar

A

non polar so less soluble in aqueous solutions

22
Q

examples where non polar amino acids in protein are used for structural purposes

A

in the centre of protein to stabilise
at surface of cell so in contact with membrane- glycoproteins

23
Q

what does quatenary structure refer to

A

the way the polypeptides fit together when there is more than one polypeptide in a protein

23
Q

example of a protein that has a quaternary structure

A

haemoglobin - it is a conjugated protein-4 polypeptide chains and 4 heme groups

23
Q

where are polar amino acids found in the cell

A

on surface of membrane because they can interact with water molecules
line pores in membrane creating hydrophilic channels for transport of polar molecules

24
Q

what is a conjugated protein

A

a protein with one or more non protein groups

25
Q

examples of non conjugated proteins

A

insulin and collagen

26
Q

what does insulin consist of

A

2 chains of amino acids joined by disulfide bridges (21+32)
forms 2 quaternary structures- dimers and hexamers which as as storage molecules

27
Q

what does collagen consist of

A

a fibrous protein with 3 polypeptide chains held by hydrogen bonds (which allow for good tensile strength) in a helix shape

28
Q

where does the hydrogen bonding in the secondary structure occur

A

between the amino and carboxyl groups

29
Q

example of globular protein

A

insulin also functions as hormone

30
Q

what does insulins properties allow for

A

its small size and hydrophilic surface allows it to be dissolved in blood plasma
shape allows it to bind to specific receptor protein

31
Q

what are fibrous proteins

A

long strands of polypeptide chains that have cross linkages due to hydrogen bonds

32
Q

where can collagen be found

A

it has a flexible structure so forms connective tissues- tendons, ligaments, bones, skin

33
Q

shape of globular proteins

A

roughly circular

34
Q

shape of fibrous proteins

A

long strands

35
Q

amino acid sequence in globular

A

irregular and wide range of r groups

36
Q

amino acid sequence

A

repetitive with a limited range of r groups

37
Q

function of globular

A

physiological/functional

38
Q

function of fibrous

A

structural

39
Q

examples of globular

A

haemoglobin, enzymes, insulin, immunoglobin

40
Q

examples of fibrous

A

collagen, keratin, myosin, actin, fibrin

41
Q

solubility of globular

A

generally soluble in water

42
Q

solubility of fibrous

A

generally insoluble in water