Amino Acids And Proteins Flashcards

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1
Q

Describe the general structure of an amino acid

A

CHIRAL CARBON with 4 distinct groups:

  • H
  • NH2 at N terminal
  • COOH at C terminal
  • R group (different for each AA)
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2
Q

Which sterioisomer is naturally found in amino acids and why?

A
  • TRANS (L-form)

- Cannot be superimposed

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3
Q

What does the solubility of a protein depend on?

A
  • POLARITY

- Ability to form hydrogen bonds with water molecules

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4
Q

Define AMPHIPATHIC and explain how amphipathic molecules behave in aqueous solution

A
  • Amphipathic molecules have both POLAR AND NON-POLAR regions
  • In aqueous solution hydrophobic non polar regions cluster together and hydrophilic polar molecules interact with water
  • FORMATION OF A MICELLE
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5
Q

Give 5 examples of the roles of proteins in the body

A
  • Biological catalysts (e.g. Enzymes)
  • Structural support (e.g. Collagen)
  • Ion channels (e.g. Na+ channels in plasma membrane)
  • Transporters (e.g. Haemoglobin)
  • Receptors (e.g. Hormones, neurotransmitters)
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6
Q

Explain how an amino acid can be ionised

A
  • ZWITTERION
  • When placed in acidic solution -NH2 —> -NH3+
  • When placed in alkali solution -COOH —> -COO-
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7
Q

Describe how amino acids can be classified

A
  • Classified according to chemical properties of R groups

- Non polar, Polar (uncharged) and Polar (charged)

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8
Q

Describe the features of a NON-POLAR amino acid

A
  • HYDROPHOBIC
  • Overall charge = 0
  • Can be aliphatic or aromatic
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9
Q

Give 5 examples of non-polar amino acids

A
  • Glycine
  • Leucine
  • Phenylalanine
  • Tryptophan
  • Valine
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10
Q

What is the difference between ALIPHATIC and AROMATIC?

A
  • ALIPHATIC molecules consist of long chain/branched hydrocarbons
  • AROMATIC molecules contain a benzene ring
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11
Q

How can some molecules be polar but have no overall charge?

A
  • Contain polar groups that can interact with water

- Big bulky side chains

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12
Q

Give 5 examples of POLAR, UNCHARGED amino acids

A
  • Serine
  • Asparagine
  • Tyrosine
  • Threonine
  • Cysteine
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13
Q

Give 5 examples of POLAR, CHARGED amino acids and state their overall charge

A
  • Lysine (+ve)
  • Histindine (+ve)
  • Arginine (+ve)
  • Aspartate (-ve)
  • Glutamate (-ve)
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14
Q

Explain how the pH of a solution will affect the structure of the amino acid

A
  • pH > pKa then amino acid group will be DE-PROTONATED

- pH

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15
Q

Describe the formation of a peptide bond

A

CONDENSATION REACTION of -COOH group on one amino acid and -NH2 group on another amino acid

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16
Q

What are the properties of a peptide bond?

A
  • Rigid
  • Planar
  • COVALENT
17
Q

Define the ISOELECTRIC POINT (pI) of a protein

A

pH at which the protein has NO OVERALL NET CHARGE

18
Q

How could you predict the overall net charge of a protein at physiological pH (7)?

A
  • pH > pI protein will be DE-PROTONATED so will be -ve charged (ACIDIC)
  • pH
19
Q

Name 4 types of intermolecular forces commonly found in biological molecules

A
  • Hydrogen bonding
  • Ionic bonding
  • Van der Waals forces
  • Hydrophobic interactions
  • (Disulphide bonds - between cysteine residues)
20
Q

What is meant by a CONJUGATED PROTEIN?

A

Contains COVALENTLY LINKED chemical components in addition to amino acids e.g. Haem groups in haemoglobin, lipids in lipoproteins