1.3 - Proteins Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

Explain briefly what proteins are

A

A diverse group of large complex polymers made up of amino acids (after water, they are the most abundant molecules in the body)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What type of functions do proteins have? (hint - there are 5)

A
  • Structural
  • Catalytic
  • Signalling
  • Transport & storage
  • Defense
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is the structural function of a protein?

A

Proteins are the main component of body tissues (e.g muscle, skin, ligaments & hair)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is the catalytic function of a protein?

A

All enzymes are proteins, catalysing many biochemical reactions - used for speeding up certain chemical reactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the signalling function of a protein?

A

Many hormones & receptors are proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What is the transport & storage function of a protein?

A

Proteins are a major element in the transport & storage of certain molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is the defense function of a protein?

A

Protection against disease - all antibodies are proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Name the main parts in the general structure of a protein

A
  • Amino group
  • Carboxyl group
  • Side chain a.k.a R group (only part of an amino acid that differs between each - defines an amino acid)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Describe how a peptide bond is formed

A
  • From a condensation reaction
  • The -OH from carboxyl group of one amino acid & -H from the other amino acid’s amine group
  • Form covalent (peptide) bond
  • Release a water molecule
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Name the structural order of proteins

A

Primary structure -> Secondary structure -> Tertiary structure -> Quaternary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Describe the primary structure of a protein

A
  • unique sequence of amino acids

- determined by inherited genetic info

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Describe the secondary structure of a protein

A
  • Found in most proteins

- Consists of coils & folds in the polypeptide chain from H bonding between parts of the polypeptide backbone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Name the two types of secondary structure of a protein

A
  • Alpha helix (coiled)

- Beta pleated sheet (folded)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Describe the tertiary structure of a protein

A
  • Elements of secondary structure come together to form a 3D fold
  • Overall shape of a polypeptide, results mainly from interactions between R groups
  • Interactions include: H bonds, ionic bonds, hydrophobic interactions, Van Der Waals interactions & disulphide bridges
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What are disulphide bridges?

A

Strong covalent bonds that may reinforce protein structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Describe the quaternary structure of a protein

A

When two or more polypeptide chains form one subunit

17
Q

Name two common examples of proteins that have quaternary structure

A
  • Collagen

- Haemoglobin

18
Q

Name the 5 factors that affect the protein structure

A
  • Primary structure

Physical & chemical conditions e.g:

  • Changes in pH
  • Salt concentration
  • Temperature
  • Other environmental factors that can cause protein to unravel
19
Q

What does it mean when a protein has denatured?

A
  • The protein has lost its original structure & has become biologically inactive
20
Q

Describe the general structure of a globular protein & how this affects its function

A
  • Usually have a spherical shape caused by tightly folded polypeptide chains
  • Chains are usually folded so that hydroPHOBIC groups are on the INside, while hydroPHILIC groups are in the OUTside
  • This allows many of them to be soluble in water
21
Q

What are the 3 main functions of globular proteins?

A

Transport:

  • Proteins
  • Enzymes
  • Hormones
22
Q

Give an example of a globular transport protein & where they are found

A
  • E.g haemoglobin & myoglobin

- These proteins are embedded in membranes

23
Q

Give an example of a globular enzyme

A
  • Lipase

- DNA polymerase

24
Q

Give an example of a globular hormone

A
  • Oestrogen

- Insulin

25
Q

Describe the general structure of a fibrous protein & how this affects its function

A
  • Formed from parallel polypeptide chains held together by cross-links
  • These form long, rope-like fibres w/ high tensile strength
  • Generally insoluble in water
26
Q

Name 3 common examples of fibrous proteins

A
  • Collagen
  • Keratin
  • Silk
27
Q

Give the use of collagen

A

Main component of connective tissue (e.g ligaments, tendons, cartilage)

28
Q

Give the use of keratin

A

Main component of hard structures (e.g hair, nails, claws & hooves)

29
Q

Give an example of the use of enzymatic proteins

A

In digestion, to hydrolyse bonds in food molecules

30
Q

Give an example of the use of storage proteins

A
  • Casein (protein of milk) is the main source of amino acids for a baby
  • Plants have storage proteins in their seeds. Ovalbumin (protein of egg white) is used as an amino acid source for the developing embryo
31
Q

Give an example of the use of defensive proteins

A

Antibodies inactivate & help destroy pathogens

32
Q

Give an example of the use of transport proteins

A
  • Haemoglobin (iron-containing protein & found in blood) transports O2 from lungs to other parts of body
  • Other transport proteins transport molecules across membranes