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1.1 Cell Biology > Proteins > Flashcards

Proteins Flashcards

1
Q

What are the monomers of proteins?

A

Amino acids

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2
Q

What are polymers of amino acids?

A

Polypeptides

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3
Q

What is the protein that plays a structural role in hair?

A

Keratin

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4
Q

What is the protein that plays a structural role in clotting?

A

Fibrin

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5
Q

What gives proteins a structural function?

A

Their rigid structure

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6
Q

What are enzymes?

A

Biological catalysts that accelerate chemical reactions

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7
Q

What is essential for protein structure?

A

3D shape

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8
Q

What must be correct for the correct structure?

A

Protein transcript

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9
Q

How does a transport protein work?

A

Large molecules pass through the membrane through active transport which causes the protein to flip

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10
Q

What is a channel protein?

A

Specific ions bind to receptors and the molecule is allowed through

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11
Q

What do membrane proteins allow?

A

Transport of polar substances through the phospholipid bilayer through diffusion and active transport

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12
Q

What transports iron in the body?

A

Transferrin

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13
Q

What transports oxygen around the body?

A

Haemoglobin

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14
Q

What transports oxygen to muscles?

A

Myoglobin

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15
Q

What shape protein is essential for transport?

A

Globular

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16
Q

What type of protein is part of the immune system?

A

Antibodies

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17
Q

How do antibodies function?

A

They recognise foreign substances and induce an immune response

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18
Q

How do muscles contract?

A

The sliding action between filaments of actin & myosin

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19
Q

An example of a protein that contracts in the digestive tract?

A

Cilia

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20
Q

An example of a protein that contracts during mitosis?

A

Spindle fibres

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21
Q

What proteins are intercellular messengers?

A

Hormones

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22
Q

What do hormones do?

A

Influence the metabolism of cells

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23
Q

How does insulin enter cells?

A

Receptor protein reacts with insulin & opens channel proteins for glucose to enter cells

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24
Q

Name an enzyme involved in the glycolytic pathway

A

Glycogen synthase

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25
Name an enzyme involved in DNA replication
DNA polymerase
26
Name an enzyme that allows lactose to cross cell membrane
Lactose permease
27
Name a structural protein found in connective tissue
Collagen
28
Name 3 proteins involved in the immune system
Antibodies, cytokines & chemokines
29
Name 3 parts of an amino acid attached to the planar carbon
Amino group, R side chain & carboxyl group
30
What is the only difference between amino acids
The R side chain
31
What does the R side chain influence?
How the protein folds & its 3D structure
32
How many distinct amino acids are there?
20
33
Name 2 subdivisions of amino acids
Hydrophobic and Hydrophilic
34
Name some characteristics of hydrophobic amino acids
Repel aqueous solution, reside on the interior of proteins, doesn't ionise or form hydrogen bonds
35
Name some characteristics of hydrophilic amino acids
Interact with aqueous solution, reside on the exterior of proteins, form hydrogen bonds
36
What is physiological pH?
7.4
37
What charge does an amino acid have at physiological pH?
No charge
38
What name is given to the neutral charged amino acid molecule at physiological pH?
Zwitterion
39
What is the carboxyl group (COOH) converted to at physiological pH?
COO-
40
What is the amine group (NH2) converted to at physiological pH?
NH3+
41
Which of the groups of an amino acid is acidic?
The carboxyl group
42
Which of the groups of an amino acid is basic?
The amino group
43
What happens if you increase the pH of an amino acid solution?
A proton from the amino group will bond with a hydroxide ion to form water molecules and the amino acid is given a negative charge
44
What happens if you decrease the pH of an amino acid solution?
A proton will bond with the carboxyl group and the molecule will be given a positive charge
45
When the net charge of an amino acid is 0, the pH is said to be...
Isoelectric point (pI)
46
Non-polar aliphatic amino acids
Glycine, alanine, valine, leucine, methionine, isoleucine
47
Polar & uncharged amino acids
Serine, threonine, cysteine, proline, asparagine, glutamine
48
Aromatic amino acids
Phenylalanine, tyrosine, tryptophan
49
Positively charged amino acids
Lysine, arginine, histidine
50
Negatively charged
Aspartate, glutamate
51
What is primary structure?
Specific sequence of amino acids joined by peptide bonds
52
What is the free amino group called in the primary structure?
N terminus
53
What is the free carboxyl group called in the primary structure?
C terminus
54
What is secondary structure?
Local foldings of chains of amino acids
55
Name the 2 types of secondary structure
Alpha helix & beta pleated sheets
56
What holds the secondary structure in place?
Hydrogen bonds
57
What atoms form hydrogen bonds with each other during secondary structure?
The carbonyl O and an amino H
58
What bonding pattern causes the alpha helix structure?
The carbonyl O in the backbone bonds with the H of an amino group 4 amino acids down
59
What type of bonding causes beta pleated sheets?
When a peptide chain turns back on itself or if 2 chains line up close to each other
60
What is tertiary structure?
The 3D structure of a protein
61
Do all proteins have quaternary structure?
No
62
What is quaternary structure?
Polypeptides join together
63
How many peptide chains in haemoglobin?
4
64
How many peptide chains in DNA polymerase?
10
65
What is denaturation?
Protein loses its higher order structure but not primary structure
66
What causes denaturation?
Inappropriate heat, pH, and chemical reactions
67
What is the name given to a denatured protein that regains its shape
Renatured
68
What type of reaction forms peptide bonds?
Condensation dehydration
69
What molecule is lost in a condensation dehydration reaction?
Water

1.1 Cell Biology (9 decks)

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