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Molecules, Genes and Disease - Semester 1 > Week 1 - Amino acids and Proteins > Flashcards

Week 1 - Amino acids and Proteins Flashcards

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Organic Chemistry 101 flashcards
1
Q

Functions of lysosomes

A
  1. Cellular digestion: intracellular, contain hydrolytic enzymes
  2. Degrade certain macromolecules
  3. Phagocytose particulate matter
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2
Q

Functions of Golgi complex

A
  1. Export of proteins

2. Packages and modifies macromolecules synthesised on the surface of RER

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3
Q

Functions of mitochondria

A
  1. ATP synthesis

2. Generate heat in brown fat instead of ATP

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4
Q

Functions of nucleus/nucleolus

A
  1. RNA synthesis
  2. DNA synthesis and repair
  3. RNA processing and ribosome assembly (nucleolus)
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5
Q

Functions of plasma membrane:

A
  1. Cell morphology and movement
  2. Transport of ions and small molecules
  3. Selective structural barrier
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6
Q

Functions of cytoplasm

A
  1. Metabolism of carbohydrates, amino acids and nucleotides

2. Fatty acid synthesis

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7
Q

Name the bonds important for macromolecular structure.

A
  1. Hydrogen bonds: between neutral groups/ between peptide bonds
  2. Ionic interactions: attraction/repulsion
  3. Hydrophobic interactions
  4. Van der Waals interactions: any 2 atoms in close proximity
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8
Q

Explain the differences between hydrophobic and hydrophilic molecules in water.

A

Hydrophilic molecules from hydrogen bonds and dissolve.

Hydrophobic molecules cannot form hydrogen bonds and are insoluble.

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9
Q

Explain the concept of pH.

A

pH is the concentration of protons in aqueous solution.

pH= -log(H+)

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10
Q

Explain the concept of pK.

A

pH = pKa + log[A-]/[HA]

The larger the Ka, the stronger the acid.

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11
Q

Buffers

A

A buffer is a solution that resists change in pH following the addition of an acid or base.
A buffer can be created by mixing a weak acid with its conjugate base.
Maximum buffering capacity: pH = pKa
If [HA] = [A-], pH = pKa

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12
Q

List all non-polar amino acids.

A
  1. Glycine
  2. Alanine
  3. Valine
  4. Leucine
  5. Isoleucine
  6. Methionine
  7. Proline (non-polar aliphatic)
  8. Phenylalanine, Tryptophan (non-polar aromatic)
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13
Q

List all polar uncharged amino acids.

A
  1. Serine
  2. Threonine
  3. Asparagine
  4. Glutamine
  5. Tyrosine
  6. Cysteine
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14
Q

List all polar, positively charged amino acids.

A
  1. Lysine
  2. Arginine
  3. Histidine
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15
Q

List all polar, negatively charged amino acids.

A
  1. Aspartate

2. Glutamate

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16
Q

How is the charge on an amino acid affected by pH?

A

If pH of the solution group will be protonated.

If pH of the solution > pK value –> group will be deprotonated.

17
Q

List the key features of a peptide bond.

A
  1. Partial double-bond character (shorter than a single bond)
  2. Rigid and planar –> prevents free rotation around the bond between the carbonyl carbon and the nitrogen of the peptide bond.
  3. Almost always a trans bond: mostly because of steric interference of R groups when in cis position
18
Q

Motifs

A

Folding patterns containing 1 or more elements of secondary structure

19
Q

Types of motifs

A
  1. B-alpha-beta loop

2. Beta-barrel

20
Q

Domains

A

-Part of a polypeptide chain that fold into a distinct shape
-Often has a specific functional role
Example: calcium binding domains of troponin C

21
Q

Factors that can cause denaturation

A
  1. Heat: increased vibrational energy
  2. pH: alters ionization states of amino acids; changes ionic and hydrogen bonds
  3. Detergents and organic solvents: disrupt hydrophobic interactions
22
Q

Amyloid fibres

A

-Misfolded, insoluble form of a normally soluble protein
-Highly ordered with a high degree of beta sheet
-Core beta sheet forms before the rest of the protein
-

23
Q

How many amino acids are there in one turn of an alpha-helix?

A

3.6

24
Q

How many base pairs are there in one turn of a DNA double helix?

A

10

25
Q

State the features of fibrous proteins.

A
  1. Long strands and sheets
  2. Usually no tertiary structure
  3. Single type of repeating secondary structure
  4. Usually insoluble
  5. Often have a structural role
26
Q

State the features of globular proteins.

A
  1. Compact shape
  2. Complex tertiary structure
  3. Several types of secondary structure
  4. Usually soluble
  5. Many different roles

Molecules, Genes and Disease - Semester 1 (6 decks)

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