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
example of a protein that has a quaternary structure
haemoglobin - it is a conjugated protein-4 polypeptide chains and 4 heme groups
23
where are polar amino acids found in the cell
on surface of membrane because they can interact with water molecules line pores in membrane creating hydrophilic channels for transport of polar molecules
24
what is a conjugated protein
a protein with one or more non protein groups
25
examples of non conjugated proteins
insulin and collagen
26
what does insulin consist of
2 chains of amino acids joined by disulfide bridges (21+32) forms 2 quaternary structures- dimers and hexamers which as as storage molecules
27
what does collagen consist of
a fibrous protein with 3 polypeptide chains held by hydrogen bonds (which allow for good tensile strength) in a helix shape
28
where does the hydrogen bonding in the secondary structure occur
between the amino and carboxyl groups
29
example of globular protein
insulin also functions as hormone
30
what does insulins properties allow for
its small size and hydrophilic surface allows it to be dissolved in blood plasma shape allows it to bind to specific receptor protein
31
what are fibrous proteins
long strands of polypeptide chains that have cross linkages due to hydrogen bonds
32
where can collagen be found
it has a flexible structure so forms connective tissues- tendons, ligaments, bones, skin
33
shape of globular proteins
roughly circular
34
shape of fibrous proteins
long strands
35
amino acid sequence in globular
irregular and wide range of r groups
36
amino acid sequence
repetitive with a limited range of r groups
37
function of globular
physiological/functional
38
function of fibrous
structural
39
examples of globular
haemoglobin, enzymes, insulin, immunoglobin
40
examples of fibrous
collagen, keratin, myosin, actin, fibrin
41
solubility of globular
generally soluble in water
42
solubility of fibrous
generally insoluble in water