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AH Biology > Unit 1.2c(i) > Flashcards

Unit 1.2c(i) Flashcards

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1
Q

What are some examples of what proteins function as?

A
  • enzymes
  • hormones
  • antibodies
  • regulators
  • transporters
  • structural proteins (form skin, hair etc)
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2
Q

What do polymers of amino acids make?

A

Monomoers

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3
Q

How many amino acids are there?

A

20

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4
Q

What does amino acid structure determine?

A

Proteins structure

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5
Q

What are R-groups?

A

Amino acid side groups

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6
Q

Do all R groups have the same functional groups?

A

No they all have different functional groups

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7
Q

What are the 4 groups that amino acids R groups fall into?

A
  • Basic (+ charge)
  • Acidic (- charge)
  • Polar
  • Hydrophobic
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8
Q

What are R group’s important for?

A

The protein function

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9
Q

What gives amino acids their unique chemical properties and their specific shapes?

A

R groups

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10
Q

What determines how proteins fold and interact?

A

R groups

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11
Q

What do basic r-groups have?

A

NH2

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12
Q

If the r-group is basic what can it accept and why?

A

It accepts H+/protons because of its NH2 becoming NH3+

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13
Q

Why would basic r groups become hydrophilic?

A

If they accept a proton

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14
Q

What group do acidic R groups have?

A

They have carboxylic acidic groups, COOH

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15
Q

Do acidic R groups gain or donate proteins/H+ ions?

A

They donate to other atoms

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16
Q

What is formed when acidic r groups donate a proton?

A

The become COO-

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17
Q

What halogens to acidic r groups when they donate a proton?

A

They become negatively charged and strongly hydrophilic

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18
Q

Are polar r groups hydrophilic or hydrophobic?

A

Hydrophilic

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19
Q

Why are polar r groups hydrophilic?

A

They form weak hydrogen bonds with water molecules

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20
Q

Why do polar R groups look for water contact?

A

They have a more positive and negative side

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21
Q

What do polar groups have on the side of their r side chains?

A

Oxygen, nitrogen and sulfur

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22
Q

What is the simplest of amino acid r groups?

A

Hydrophobic

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23
Q

What do hydrophobic R groups not contain?

A

OH, COOH, NH2, SH

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23
Q

Is hydrophobic polar or non polar?

A

Non polar

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24
Q

Do hydrophobic R groups ever develop a charge?

A

They don’t become charged

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25
Q

Is hydrophobic water loving or water hating?

A

Water hating

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26
Q

What are the 4 levels of proteins?

A

Primary, Secondary, Tertiary, Quaternary

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27
Q

What is the primary amino acid structure?

A

The order in which amino acids are synthesised during translation into the polypeptide

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28
Q

What do peptide bonds do?

A

They join the amino acids together that make the protein

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29
Q

How are peptide bonds formed?

A

Condensation reactions between carboxylic groups and amine groups on neighbouring amino acids

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30
Q

What does the carboxylic acid loose when it makes a condensation reaction?

A

OH

31
Q

What does the amine group lose in a condensation reaction?

A

H

32
Q

How is the amino acid group extended?

A

By the continuous addition onto the end of the chain

33
Q

What is the amine end and the carboxylic acid end called?

A

The N and C terminus

34
Q

What are amino acid names represented by?

A

Their 3 letter abbreviations

35
Q

What forms the secondary structures?

A

Hydrogen backbones

36
Q

What are the secondary structures called?

A
  • a-helices
  • parallel, antiparallel B-sheets, or turns
37
Q

How do secondary structure 3-d shaped form?

A

The backbone folds

38
Q

What does an a-helix secondary structure look like?

A

Spirals

39
Q

What sticks out the the a-helix?

A

R-groups stick out

40
Q

Why do a-helix’s form their specific shape?

A

Because hydrogen bonds form between the 4th peptides (between oxygen of carboxy and hydrogen of the amine)

41
Q

How are the peptide bonds formed in the a-helix?

A

The weak positive hydrogen is attracted to the weak negative oxygen

42
Q

How many amino acids are in each turn of the a-helix turn?

A

3.6

43
Q

How many amino acids are in a typical section of an a-helix?

A

11 amino acids

44
Q

Why are the R-groups free to interact?

A

Because they face outwards

45
Q

How are beta pleated sheets formed?

A

Hydrogen bonds form between parts of the polypeptide stands running next to each other

46
Q

Are the hydrogen-oxygen bonds the same as they are in the a-sheet?

A

Yes

47
Q

Where do the R-groups sit on the beta pleated sheet?

A

Above and below

48
Q

What direction do beta pleated sheets usually run in?

A

Antiparallel (opposite directions)

49
Q

What determines how antiparallel structures run?

A

Where the N and C terminal are

49
Q

What do turns do?

A

Reverse the polypeptide direction

50
Q

What do turns allow?

A

Interactions between secondary structure elements

51
Q

What is the tertiary structure?

A

The complex 3D conformation that the final polypeptide structure takes

52
Q

What interactions establish the tertiary structures?

A

Interactions between amino acid R groups

53
Q

How do prosthetic groups improve tertiary structures?

A

By giving an added function

54
Q

What are the 6 interactions tertiary structures undergo?

A

Hydrogen Bonds
Disuphilde Bridges
Ionic Bonds
Hydrophobic Interactions
London Dispersion Forces
Van de Waals Interactions

55
Q

How is a hydrogen bond formed?

A

Formed by hydrogen and oxygen atoms from the main chain and R groups

56
Q

How are disulphide bridges formed?

A

They’re formed if the R-groups in two amino acids contain a sulphur atom and are near each other

57
Q

How are ionic bonds formed?

A

They’re formed in solutions of carboxylic acid and amino groups that form charged groups in a solution. If the charges are opposite an ionic bind will form

58
Q

How are hydrophobic interactions formed?

A

They are formed when hydrophobic R groups cluster towards the interior of the protein molecule

59
Q

What are LDFs?

A

They are temporary attractive forces that individually weak but collectively contribute to maintaining protein structure

60
Q

What are van de Waals interactions?

A

they are electrical interactions between 2+ atoms/molecules that are very close to each other

61
Q

Are van de Waals weak or strong interactions?

A

They are both;

Weak by themselves
Strong when working together

62
Q

Wha quaternary structures?

A

They are several connected polypeptide sub-units that exist in proteins and are held together by tertiary interactions

63
Q

What happens if a protein only contains 1 polypeptide subunit?

A

No quaternary structure it formed, it stops at the tertiary structure.

64
Q

Haemoglobin in a quaternary structure, how many polypeptide subunits is it made of?

A

4

65
Q

Are prosthetic groups added to quaternary structures?

A

Yes they are

66
Q

Wha are prosthetic groups?

A

They are additional non-protein structures with no necessary functions

67
Q

What’s an example of a non-prosthetic group and where can it be found?

A

Haem found in Haemoglobin

68
Q

What does Haem contain?

A

An iron atom for oxygen binding

69
Q

How is iron bound to Haemoglobin?

A

It is covalently bound due to histidine amino acids

70
Q

What are the two main factors that impact protein structure?

A

Temperature and pH

71
Q

What happens to a protein when it denatures?

A

It looses its shape and function

72
Q

What influences R-group interactions?

A

Temperature and pH

73
Q

What is impacted when temperature increases?

A

First weak then strong covalent bonds are disrupted

74
Q

What does the alteration of pH from optimum result in?

A

The ionic intercations between R-groups becoming lost

AH Biology (51 decks)

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