DD - Protein Structure (3) Flashcards

1
Q

What is protein modification and when does it occur?

A
  • Covalent processing events that change the properties of a protein by proteolytic cleavage and adding a modifying group
  • Occur during post translation
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2
Q

What are the 7 main types of modification?

A
  1. Glycans (Carbohydrates)
  2. Phosphates
  3. Palmitoylation (Lipids)
  4. Proteins (Ubiquitin)
  5. Methylation
  6. Acetylation
  7. Proteolytic maturation
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3
Q

What is glycosylation?

A

Addition of complex carbohydrate group

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4
Q

What does protein glycosylation control? (6 things)

A
  1. Cellular pathways
  2. Protein trafficking
  3. Cell adhesion
  4. Host-pathogen interaction
  5. Protein stability/folding
  6. Protection against proteases
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5
Q

What is phosphorylation? and what is it important for?

A
  • A process in which a phosphate group is added to a molecule, such as a sugar or a protein
  • Important in downstream signalling
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6
Q

What proteins add phosphate groups and which remove phosphate groups?

A

Kinases add phosphate groups
Phosphatases remove phosphate groups

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7
Q

What is palmitoylation?

A

Addition of long lipid groups (help anchor proteins in membrane)

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8
Q

What amino acids can palmitoylation occur?

A

Cysteine, Glycine and Lysine

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9
Q

What is ubiquitination and degradation?

A

Proteins are marked for degradation by the attachment of ubiquitin to the amino group of the side chain of a lysine residue

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10
Q

What is methylation?

A

Addition of a -CH3 group to a protein
Occurs in lysine

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11
Q

What is acetylation?

A

Addition of an acetyl group to an organic chemical compound
Occurs in lysine

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12
Q

What is proteolytic cleavage?

A

The process of breaking the peptide bonds between amino acids in proteins

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13
Q

What happens from
Pre-proinsulin –> Proinsulin –> Insulin

A

Pre-proinsulin –> Proinsulin
- Cleavage of signal peptide
- Oxidation of disulfide bridges
Proinsulin –> Insulin
- Cleavage of C-peptide

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14
Q

How are peptide bonds broken?

A

Broken by hydrolsis by boiling in 6M acid

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15
Q

Name the 4 main prosthetic groups?

A
  1. Haem
  2. Lipid
  3. Metal ion
  4. Nucleic acid
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16
Q

What is the quartenary structure?

A

The arrangement of more that one protein molecule in a multi-subunit complex

17
Q

What are the 2 main interactions involved in the Oligomeric interaction of proteins?

A
  • Electrostatic/Polar
  • Hydrophobic