Proteins Flashcards

1
Q

What is the structure of an amino acid?

A

Central carbon atom, covalently bound to

  • Amino group
  • Carboxyl group
  • Hydrogen atom
  • R group (side chain)
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2
Q

How do amino acids ionise?

A

Amino group gains hydrogen ion
NH2 + H+ —–> NH3+

Carboxyl group gives up hydrogen ion
COOH —–> COO- + H+

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3
Q

Which group in the amino acid is acidic?

A

The carboxyl group

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4
Q

Which group in the amino acid is basic?

A

The amino group

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5
Q

How are amino acids classified? Why?

A

Based on the properties of the R groups

Because in polypeptide chains, only the hydrogen atom and the R group of the amino acids remains

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6
Q

What is an amino acid residue?

A

What remains of an amino acid after it has been jointed to another amino acid

  • R group
  • hydrogen atom
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7
Q

What are the types of properties of the R group?

A

Chemical properties

Physical properties

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8
Q

What are the possible chemical properties of the R group?

A

Polar/non-polar

Hydrophobic/hydrophilic

Acidic/basic/neutral

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9
Q

What are the possible physical properties of the R group?

A

Aliphatic/aromatic

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10
Q

What does the pKa value of amino acids measure?

A

How acidic the amino acids are

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11
Q

What does a low pKa value mean?

A

The amino acid is more acidic

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12
Q

What does a high pKa value mean?

A

The amino acid is less acidic

more basic

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13
Q

What happens to the amino acid if pH > pKa? Why?

A

Higher pH means fewer hydrogen ions present
amino acid gives up hydrogen ions
becomes deprotonated

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14
Q

What happens to the amino acid if pH < pKa? Why?

A

Lower pH means more hydrogen ions present
amino acid takes up hydrogen ions
becomes protonated

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15
Q

What is physiological pH?

A

7.4

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16
Q

What is the primary structure of a protein?

A

Amino acids joined together in a linear chain

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17
Q

What reaction occurs when two amino acids are joined together?

A

amino acid1 + amino acid 2 —–> polypeptide + water

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18
Q

What bond joins two amino acids together?

A

Peptide bond

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19
Q

What is the amino terminus of a polypeptide?

A

The amino group NH2 end of the polypeptide chain

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20
Q

What is the carboxyl terminus of a polypeptide?

A

The carboxyl group COOH end of the polypeptide chain

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21
Q

What are the properties of peptide bonds?

A

Planar

Rigid

Trans conformation

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22
Q

What is meant by peptide bonds being planar?

A

The central carbon atom
N-H
C=O

are all in the same plane

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23
Q

What is meant by peptide bonds being rigid?

A

No rotation about the peptide bond

24
Q

What atoms are involved in a peptide bond?

A

C-N

C from C=O
N from N-H

25
What is meant by the peptide bond having a trans conformation?
Heavier groups are on opposite sides of the peptide bond | the heavier groups are the central carbon atom, R group, H atom altogether
26
What is the importance of the amino acid sequence in the primary structure?
Determines the way the polypeptide chain folds the structure of the protein and hence its function
27
What are peptides/oligopeptides?
Chains of a few amino acids joined together
28
What are polypeptides/proteins?
Chains of many amino acids joined together
29
What type of bond is a peptide bond?
Covalent bond
30
What is the secondary structure?
The spatial arrangement of the polypeptide backbone
31
What are the types of secondary structures?
Alpha helix Beta strand
32
What do layers of beta strands form?
Beta pleated sheet
33
What holds the alpha helix and the beta pleated sheets together?
Hydrogen bonds between C=O and N-H
34
What are the types of beta sheets? What do they each mean?
Parallel - run in same direction Anti parallel - run in opposite directions
35
How does the polypeptide chain fold up into an alpha helix or beta pleated sheet if peptide bonds are rigid?
Bonds next to peptide bonds are free to rotate
36
What is the tertiary structure?
Secondary structure folds up to form a 3D conformation
37
What are the types of tertiary structures? What do they each mean?
Globular - spherical shape Fibrous - long strand-like shape
38
What is the general function of fibrous proteins?
Structural support Maintain shape
39
How many types of secondary structures are there in fibrous proteins?
Single repeating secondary structure
40
How many types of secondary structures are there in globular proteins?
Several different types
41
What is a classic example of a fibrous protein?
Collagen
42
What is a protein domain?
Part of polypeptide chain that folds into a distinct shape | has a specific function
43
How do water-soluble proteins generally fold up?
Non-polar hydrophobic side chains are buried within Polar/charged hydrophilic side chains are on surface
44
How do integral membrane proteins generally fold up? Why?
Non-polar hydrophobic chains are on the surface interact with hydrophobic tails Polar/charged hydrophilic chains form a channel within interact with water in and out of cell
45
What is the quarternary structure?
Different polypeptide chains coming together to form a multi-subunit protein
46
What is an example of a protein with a quarternary structure?
Hb
47
What is an example of a protein with a tertiary structure?
Myoglobin
48
What does pI stand for?
Isoelectric point
49
What is the pI of proteins?
pH at which protein has no overall charge
50
Do acidic proteins have a low or high pI value? Why?
Low | low pH means more hydrogen ions, neutralises negative charge of acidic amino acid
51
Do basic proteins have a low or high pI value? Why?
High | high pH means fewer hydrogen ions, because already have positively charged amino acids
52
What happens to the protein if pH > pI? Why?
High pH means fewer hydrogen ions amino acid gives up hydrogen ions becomes deprotonated
53
What happens to the protein if pH < pI? Why?
Low pH means more hydrogen ions amino acid takes up hydrogen ions becomes protonated
54
What are conjugated proteins?
Proteins covalently linked to additional chemical components that are not amino acids
55
What are some examples of roles of proteins? Give examples for some roles
Structural support e.g. collagen Enzymes e.g. hexokinase Transporters e.g. Hb Carriers, channels etc. Receptors, ligands etc.