proteins Flashcards

(46 cards)

1
Q

define polymer

A

a long chain of repeating units (monomers)

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2
Q

what is a condensation reaction?

A

a condensation reaction joins two monomers together, and water is formed as a by-product

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3
Q

what is a hydrolysis reaction?

A

a hydrolysis reaction breaks down (the covalent bonds between) polymers by adding water

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4
Q

what is a polymer made from amino acids called?

A

a protein

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5
Q

what is the bond that joins amino acids to form a protein?

A

peptide bond

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6
Q

what happens to an amino acid in an acidic environment?

A

in an acidic environment there are excess H+ ions, so the amino acid will absorb H+ and become positive (NH2 -> NH3+)

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7
Q

what are the features of a protein’s primary structure?

A

-the sequence of amino acids
-does not occur in nature
-only peptide bonds
-tells us the order of amino acids/how many there are in a chain

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8
Q

what are the features of a protein’s secondary structure?

A

-forms due to hydrogen bonds between NH3+ and COO-
-primary structure folds into alpha helices and beta pleated sheets

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9
Q

what are the features of a protein’s tertiary structure?

A

-further folding to produce a specific 3D shape
-contains disulfide bridges, ionic bonds, hydrogen bonds and hydrophobic interactions

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10
Q

what are the features of a protein’s quaternary structure?

A

-not found in all proteins
-two or more polypeptide chains attached to each other

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11
Q

where does a disulfide bridge occur?

A

between two R-groups that contain sulfur

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12
Q

where does an ionic bond occur?

A

bewteen charged R-groups

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13
Q

where does a hydrogen bond occur?

A

between polar R-groups

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14
Q

where do hydrophobic interactions occur?

A

between non-polar R-groups

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15
Q

order the bonds found in tertiary structures from strongest to weakest

A

strongest
disulfide bridge
ionic bond
hydrogen bond
hydrophobic interaction
weakest

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16
Q

what is the structure of an amino acid?

A

structure:
‘R’
|
NH2—-C—-COOH
|
H

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17
Q

what is the ‘R’ group?

A

also known as the variable group, it is different in every amino acid and causes different properties

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18
Q

what is the amino group?

A

NH2

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19
Q

what is the acid group?

A

COOH (carboxylic)

20
Q

what would happen to an amino acid in an acidic environment?

A

the amino group will absorb an H+ ion and become positive (NH3+)

21
Q

what would happen to an amino acid in an alkaline environment?

A

the acid group will lose an H+ ion and become negative (COO-)

22
Q

amino acid + amino acid = ?

A

dipeptide + water (condensation reaction)

23
Q

dipeptide + water = ?

A

2 amino acids (hydrolysis reaction)

24
Q

which bond joins two amino acids together?

25
what is a zwitterion?
one with both a positive and negative charge on a molecule
26
why are amino acids described as 'buffers'?
they prevent small changes in pH by accepting/donating H+ ions
27
what is a prosthetic group?
any non-polypeptide incorporated into the structure
28
what is the shape of a fibrous protein?
long, narrow fibres; often have repeated alpha helices or beta pleats
29
what is the purpose of a fibrous protein?
structural- muscle, bones, hair, skin
30
what is the amino acid sequence of a fibrous protein?
repeated sequence- to get the repetitive shape
31
how durable are fibrous proteins?
very durable, less affected by changes in temperature/pH
32
name some examples of fibrous proteins
collagen, keratin, silk
33
are fibrous proteins soluble or insoluble?
insoluble
34
what is the shape of globular proteins?
spherical, with no particular pattern
35
what is the purpose of a globular protein?
metabolic- used in chemical reactions in the body
36
what is the amino acid sequence of a globular protein?
irregular sequence- to get the irregular shape
37
how durable are globular proteins?
low durability: more affected by changes in temp./pH
38
name some examples of globular proteins
enzymes, hormones, antibodies, haemoglobin
39
are globular proteins soluble or insoluble?
soluble in water
40
where does protein trafficking take place?
1. nucleus 2. rough endoplasmic reticulum 3. golgi body 4. cell membrane 5. mitochondria
41
what happens in the nucleus during protein trafficking?
1. the nucleolus produces ribosomes 2. DNA contains the instructions used to make proteins 3. mRNA is a copy of these instructions 4. mRNA leaves via the nuclear pore
42
what happens in the rough endoplasmic reticulum during protein trafficking?
1. mRNA is converted into protein (primary structure) 2. protein leaves RER in a vesicle
43
what happens in the golgi body during protein trafficking?
1. protein is 'modified' into secondary, tertiary and maybe quaternary structure 2. protein exits golgi body in a vesicle
44
what happens in the cell membrane during protein trafficking?
some proteins are released from the cell (e.g. hormones + enzymes)
45
how is the mitochondria involved in protein trafficking?
protein production, packaging and transport require lots of ATP
46
what are glycoproteins?
modified proteins