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Year 1- Principles of Normal Function (FOM) > Proteins > Flashcards

Proteins Flashcards

1
Q

What is a protein?

A

A protein is a macromolecule consisting of amino acids arranged in a particular structure that enables it to carry out a specific function in a particular context

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2
Q

Proteins can be either??

A
  1. Structural
  2. Functional
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3
Q

Give an example of a structural protein.

A

Keratein in the skin which provides structure.

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4
Q

Give an example of a functional protein.

A

Enzyme to catalyse a reaction or antibody in i8mmune defence.

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5
Q

Define the process of transcription.

A

Tells cells how to make messenger RNA (mRNA)

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6
Q

Define the process of translation.

A

mRNA is used by the cell as a code to make chains of amino acids

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7
Q

How many nucleotides code for an amino acid?

A

Three

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8
Q

What can three nucleotides also code for?

A

A STOP instruction.

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9
Q

What does uracil match with?

A

Adenine.

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10
Q

How many naturally occurring amino acids are there?

A

20

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11
Q

Draw the structure of an amino acid.

A

:) not paying for pro lol so look it up xoxox

should have an amine group (NH2), R group (side chain which changes w every amino acid) and carboxylic acid group (OOH).

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12
Q

All amino acids (except one) are chiral. What does this mean and what is the one that isn’t?

A

Asymmetrical.

Glycine.

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13
Q

Amino acids can become charged.

Amino acids at a low pH can become??

A

Slightly positively charged as take up hydrogen ions.

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14
Q

Amino acids at a neutral pH have?

A

Two charges- one positive, one negative

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15
Q

Amino acids at a high pH have?

A

Slightly negative charge due to the OH.

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16
Q

What is an aliphatic amino acid and give an example.

A

‘R’ group consisting of hydrocarbon chains
E.g. glycine.

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17
Q

What is an aromatic amino acid and give an example.

A

‘R’ group consisting of hydrocarbon ring

Phenylalanine.

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18
Q

Give an example of a sulphur containing amino acid

A

Methionine

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19
Q

Give an example of a basic/acidic amino acid.

A

Basic- Lysine
Acidic- Glutamate

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20
Q

Give an example of a polar amino acid/.

A

Serine

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21
Q

Give an example of a miscellaneous amino acid.

A

Proline

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22
Q

If an amino acid has a long chain of hydrocarbons, what kind of properties does this give?

A

Hydrophobic, non-polar properties.

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23
Q

A heel prick is done in babies to look for?

A

Abnormally high amounts of the aromic amino acid, phenylalanine as may indicate phenylketonuria, a metabolic disease.

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24
Q

What can Phenylketonuria lead to?

A

Severe immune neurological damage or death.

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25
Q

The presence of sulphur in an amino acid allows what to from?

A

Disulphide bridges.

These are covalently bonded linkages which occur between two sulphur containing amino acids which helps w strength.

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26
Q

Proline is a miscellaneous amino acid. What does this mean?

A

It is unusual and doesn’t fit into any of the other groups.

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27
Q

Define the primary structure of an amino acid.

A

The sequence in which amino acid monomers are joined together to form a polypeptide chain.

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28
Q

In a chain ten aminoi acids long, how many possible combinations of amino acids could there be?

A

20 to the power of 100.

(any one of 20 amino acids could be in position one, any one of 20 amino acids could be in position two…etc all the way to 10).

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29
Q

How are two amino acids joined together to form a primary structure?

A

The formation of a peptide bond.

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30
Q

Two amino acids joined together is known as a…?

A

Dipeptide.

three would be a tripeptide etc.

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31
Q

What kind of bonding do secondary structure rely on?

A

Hydrogen bonding between the slightly negatively charged oxygen atoms in the carboxyl groups and the slightly positively charged nitrogen atoms in the amine groups.

32
Q

Name the two most common secondary structures and give an exmaple.

A

Alpha helix- myoglobin
Beta pleated sheet- porins (allow water into cells) and fatty acid binding proteins.

33
Q

Describe tertiary structures.

A

Formed when R groups interact w distant amino acids, contributing to the 3D shape.

34
Q

Functional proteins must have at least one…?

A

Tertiary structure.

35
Q

Are R groups hydrophobic or hydrophillic?

A

Can be either.

36
Q

Describe quaternary structure.

A

More than one polypeptide chain, which have already formed their own tertiary structures, come together.

37
Q

Give an example of a protein w a quaternary structure.

A

Haemoglobin

38
Q

When does denaturation occur?

A

When a protein’s chemical bonds are disrupted, or even destroyed. Biological function is lost.

39
Q

What determines the function of a protein?

A

How amino acid monomers interact w each other.

40
Q

Describe the function of structural proteins.

A

Provide support within connective tissues.

E.g. collagen, keratin.

41
Q

Describe the function of enzymatic proteins.

A

Permitting the selective acceleration of chemical reactions.

e.g. digestive enzymes like amylase.

42
Q

Give an example of receptor proteins.

A

G-proteins which play a role in many physiological processes.

43
Q

Describe the function of hormonal proteins.

A

Coordinating metabolic function.

E.g. insulin.

44
Q

Give an example of storage proteins.

A

Feratin, the storage protein for iron.

45
Q

Describe the function of transport proteins.

A

Responsible for transporting resources.

E.g. haemoglobin.

46
Q

Describe the function of contractile proteins.

A

Involved in movement.

E.g. actin and myelin

47
Q

Describe the function of defensive proteins.

A

Provide protection against disease.

E.g. immunoglobulins.

48
Q

After proteins have been transcribed, they may undergo?

A

A post-translational modification.

49
Q

This modification can occur at the same time as what process?

A

Translation

50
Q

Name the three types of conjugated proteins.

A

Glycoproteins, lipoproteins and metalloproteins.

51
Q

How do prorteins become conjugated proetins?

A

After undergoing post or co translational modifcation.

52
Q

What are glycoprotiens?

A

Proteins where one or more carbohydrate moleculeses are covalently attached.

53
Q

If a few carbohyrdate monomers exist together within a chain, what is this molecule known as?

A

This molecule is known as an oligosaccharide.

54
Q

Name some of the effects of glycsylation.

A
  1. Stability
  2. Solubity
  3. Cell signalling (most important)
  4. Orientation
55
Q

How can glycoproteins be used for diagnosis?

A

Pateints w undiagnosed diabetes have chronically elevated levsls of glucose in their blood. Over time, excess glucose binds to haemoglobin within erythrocytes, forming glycoproteins.
By detecting the conc of glycoproteins in blood, clinicains can see increased blood glucose.

56
Q

How are lipoproteins formed?

A

Proteins combine w lipids.

57
Q

Where are lipoproteins found?

A

In the cell membrane.

58
Q

What do lipoproteins do?

A

Transport hydrophobic molecules.

-For example, cholestrol transport in blood.

59
Q

what do apolipoproteins do?

A

Transport fats, fat soluable viatmins and fat soluable hormoes around the body within the blood and cerebral spinal fluid

60
Q

What are metalloproteins?

A

Protein molecules with metal ions within their structure.

61
Q

List some functions of metalloproteins.

A

Ezymatic, signal transduction, transport and storage.

62
Q

Describe the structure of haomoglobin.

A

Haemoglobin has a large quateranry structure consisitng of four polypeptide chains consisting of two alpha subunits and two beat subunits.

63
Q

The non polar interfaces of haemoglobin play an important role in what?

A

Transmitting info between individual subunits about their individual activities.

64
Q

Which organic molecule is found is every subunit?

A

Haem.

65
Q

How does haemoglobin transport oxygen around the body?

A

Because of the interactions between iron, the haem molecule and polypeptide subunit.

66
Q

How many molceuls of oxygen can one haemoglobin transport?

A

Four due to the four subunits.

67
Q

Sickle cell anaemia is caused by what amino acid issue?

A

Substitution of bases.

68
Q

What issues arise in individuals s w sickle shaped cells.

A

-Stuggle to pass though capillaries
-Inefficient in delivering oxygen to tissues.

69
Q

What is a bloodfilm?

A

A thin smear of whole blood, prepared and viewed under a light microscope.

70
Q

Name five functions of globular proteteins.

A

Storage, ezymatic, transport, hormones and structure.

71
Q

What are fibrous protiens?

A

Proteins w an elongated shape.

Looks like a rop

72
Q

Where are fibrous proteins commonly found?

A

Muscle fibres and connective fibres.

73
Q

What is an essential co-factor in the production of collagen?

A

Vitamin C

74
Q

What are membranous proteins?

A

Proteins embedded in cell membranes.

75
Q

What is the main function of membranous proteins?

A

Transporting molecules over cells. One example would be an aqua duct proein.

Year 1- Principles of Normal Function (FOM) (21 decks)

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