Proteins Flashcards

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1
Q

the single unit of a protein

A

amino acid

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2
Q

amino acid aka

A

residue

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3
Q

four components of an amino acid

A
  • amino group
  • carboxylic acid
  • hydrogen atom
  • variable R group / side chain
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4
Q

amphiprotic definition

A

containing both acidic and basic functional groups

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5
Q

essential

A

body cannot synthesize them

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6
Q

how many essential proteins are there?

A

8

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7
Q

what are the 4 classifications of amino acids?

A

nonpolar
polar
acidic
basic

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8
Q

acidic amino acids have

A

carboxylic acid , negative charge

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9
Q

basic amino acids have

A

amino, positive change

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10
Q

how to form a polypeptide

A

condensation reaction to join 2 amino acids

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11
Q

what does forming a polypeptide require?

A

carboxyl groups
amine

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12
Q

peptide

A

links between amino acids

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13
Q

what is the growth order for a polypeptide

A

N to C terminus

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14
Q

conformation

A

shape of a protein

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15
Q

what are the levels of a protein structure?

A

primary, secondary, tertiary, quaternary

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16
Q

primary structure

A

unique sequence of amino acids

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17
Q

how is the primary structure determined

A

by DNA

18
Q

secondary structure results from…

A

hydrogen bonds are regular intervals along the polypeptide backbone

19
Q

what are the typical shares of the secondary structure?

A

alpha helix
beta pleats

20
Q

who discovered the alpha helical structure of protein and when?

A
  • linus pauling
  • 1961
21
Q

tertiary structure describe

A

interactions between R groups

22
Q

what happens between polar bonds /charged amino acids at the tertiary structure

A

hydrogen bonds
dipole-dipole
ion-dipole

23
Q

what happens between non polar amino acids in the tertiary structure

A

hydrophic interactions

24
Q

disulfide bridge

A

formed between the sulfhydryl groups of cysteine amino acids

25
Q

proline kink

A

only amino acid where the R group is attached to the amino group creating a kinked shaped

26
Q

all proteins have tertiary structure

A
27
Q

quaternary structure

A

proteins will have a fourth level of structure that involves interactions between two or more polypeptide chains

28
Q

types of quaternary structure

A
  • fibrous
  • globular
29
Q

fibrous quarternary structure properties

A

water insoluble, threadlike

30
Q

globular quarternary structure

A

water soluble, compact spherical

31
Q

conformational change

A

change in the shape of a protein, can be reversible, doesn’t disrupt function but rather defines the function

32
Q

example of a conformational change

A

carrier protein

33
Q

denaturation

A

change in the shape of the protein that disrupts protein function

34
Q

renaturation

A

some proteins can return to their functional shape after denaturation

35
Q

Test that looks for starch

A

iodine

36
Q

test that looks for a reducing sugar

A

benedict’s

37
Q

test that looks for protein

A

Biuret

38
Q

test that looks for lipid

A

Sudan 4

39
Q

positive test colour for iodine

A

black

40
Q

positive test colour for benedict’s

A

orange

41
Q

positive test colour for bioret

A

purple

42
Q

positive test colour for sudan 4

A

red