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Biology > Proteins > Flashcards

Proteins Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

what are proteins

A

proteins are polymers made up of amino acids joined together by peptide bonds.

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2
Q

what type of reaction joins two amino acids

A

condensation

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3
Q

what is the bond between two amino acids called

A

peptide bond

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4
Q

what reaction breaks the bond between two amino acids

A

hydrolysis

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5
Q

what is the primary structure of the protein?

A

the sequence of the amino acids in the protein chains

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6
Q

two types of secondary structure that can appear in a protein

A
  1. coiled structure called alpha helix
  2. a flatter folded structure called beta beta-plated sheet
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7
Q

what bonds hold the secondary structure together.

A

hydrogen bonds

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8
Q

tertiary structure of a protein

A

the overall 3D shape of the protein

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9
Q

strength of hydrogen bond

A

individual bonds are weak but often many H bonds are formed and collectively they provide stability.

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10
Q

strength of an ionic bond

A

stronger than H bonds

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11
Q

disulfide

A

very strong

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12
Q

hydrophobic/hydrophilic interactions

A

weak interactions

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13
Q

properties of globular proteins

A

compact
water-soluble
spherically shaped

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14
Q

why are globular proteins soluble?

A

hydrophobic R groups at the centre of the protein and hydrophilic on the outside/surface so water molecules can interact with surface

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15
Q

how does globular proteins’ solubility enable them to carry out their function?

A

they can carry out important metabolic reactions in an aqueous environment

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16
Q

Examples of globular proteins

A

haemoglobin
enzymes
peptide hormones
antibodies

17
Q

T/F haemoglobin has a quaternary structure

A

TRUE

18
Q

T/F haemoglobin does not have a prosthetic group

A

FALSE - the haem group is a prosthetic group

19
Q

T/F haemoglobin is a simple protein

A

FALSE-haemoglobin is a conjugated protein because it contains a prosthetic group.

20
Q

Describe what a conjugated protein is

A

a conjugated protein has a permanent non-protein component called a prosthetic group

21
Q

why is haemoglobin described as a conjugated protein?

A

has 4 haem groups as part of its structure

22
Q

how does solubility helop globular proteins

A

insulin has to be transported in the blood to target cells, so it is important that it is soluble.

23
Q

how does a very specific 3D shape help globular proteins.

A

insulin has to bind to receptors on target cells therefore its 3D shape is very important

24
Q

what is transcription

A

the first stage of protein synthesis

25
Q

what happens during transcription

A

DNA - mRNA

26
Q

what is translation

A

the second stage of protein synthesis

27
Q

what happens during translation

A

mRNA- Protein

28
Q

role of transcription

A

to produce short single-stranded sections of mRNA using DNA as a template

29
Q

Process of transcription

A
  1. DNA helicase unwinds and unzips the DNA - breaking hydrogen bonds between nucleotide bases

2.pre-mRNA forms using complementary base pairing with the template strand of DNA

  1. RNA polymerase catalyses the formation of phosphodiester bonds in the pre-mRNA
30
Q

Why is collagen such a strong molecule

A

it is made up of three polypeptides wound together in a strong rope like structure

31
Q

describe and explain why collagen is a fibrous protein

A
  • triple helix structure
  • long polypeptide chains
  • structural role , stability within phospholipid bilayer
  • no tertiary structure
  • high number of hydrophobic R groups makes it insoluble
32
Q

why are fibrous proteins insoluble?

A

high number of hydrophobic R groups

33
Q

what are fibrous proteins?

A

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

34
Q

why are fibrous proteins suited for structural role?

A
  • insoluble
  • organised structure due to repetitive sequence
35
Q

examples of fibrous proteins

A

keratin
elastin
collagen

36
Q

what are globular proteins

A

proteins that are compact spherical and soluble in water

37
Q

why do globular proteins form a spherical shape when folding into their tertiary structure

A
  • their non-polar hydrophobic r groups are orientated towards centre of the protein
  • polar hydrophilic R groups are on outside of protein
38
Q

what does the prosthetic heam group contain in haemoglobin?

A

iron which is able to reversibly combine with an oxygen molecule

39
Q

how much oxygen can a haemoglobin carry

A

it has 4 heam groups so 4 oxygen molecules.

Biology (14 decks)

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