03. Amino acids Flashcards

1
Q

What are the 3 different ways to classify / identify amino acids?

A
  1. Based on side chain (polar, ionisable, hydrophilic / non-polar, hydrophobic) etc
  2. Based on chemical structure – aromatic / straight chain etc
  3. Essential / non-essential
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2
Q

How many standard amino acids are there, and how many are essential?

A

20, only 9 are essential

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3
Q

What is meant by essential / non-essential amino acids?

A

Essential : cannot be manufactured by the body, must be obtained by diet (meat/dairy or combination of cereals and legumes)

Non-essential : can be manufactured by the body

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4
Q

In mammalian proteins, amino acids are only in which configurationand amino group is on which side?

A

L-configuration

Which means amino group (N-terminus) is on left;

D-configuration : amino group is on right

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5
Q

Where do non-essential amino acids come from?

A

The carbon backbone of these amino acids are intermediate products from glucose undergoing glycolysis / TCA cycle

Glycolytic and TCA cycle intermediates generate the nonessential and conditionally essential amino acids.

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6
Q

What is the general formula of an amino acid?

A

NH3+ – C(H)R – COO- (zwitterion at neutral pH)

NH2 – C(H)R – COOH

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7
Q

Will the acidic or basic form of amino acids exist if:

(a) pH = pKa
(b) pH < pKa
(c) pH > pKa

A

Ka : dissociation constant of acid

(a) 50% acidic form, 50% basic form
(b) acidic form dominates
(c) basic form dominates

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8
Q

What are non-standard amino acids?

A

Amino acids which are not naturally found in proteins, and are usually modified after they are incorporated into the protein.

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9
Q

What are 2 ways in which an amino acid can be modified into a non-standard amino acid?

Hint : not the TYPES OF MODIFICATION

A
  1. After translation in the cell –> protein formed (amino acids are modified by golgi apparatus after being incoporated into protein)
  2. chemical modification(in labs etc)
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10
Q

What is the importance of non-standard amino acids in biological systems?[2]

A
  1. Some are metabolic precursors
  2. some have specific biological functions in the body.
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11
Q

what is the main purpose of modification of amino acids?

A

To increase functionality of proteins

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12
Q

Modification 1: Hydroxylation

What is hydroxylation?

Proline is an amino acid found in collagen. What is the purpose of hydroxylation of proline?

A

Replacing a hydrogen atom with –OH group

Proline has an additional OH group for hydrogen bonding, can strengthen structure of collagen and hence, tendon and tissues.

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13
Q

What is acetylation? Why is it important?

A

It is to form an amide bond at the amino group (-NH2 –> -NH=O-CH3)

It reduces positive charge of amino acids and reduces degradation of amino acids (since most amino acids need NH2 group to react)

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14
Q

What is phosphorylation? What is it significance in biological systems?

A

Replacing of -OH group to H2PO4 on serine, threonine, and tyrosine residues.

  • Phosphorylation affects protein function by activating or inactivating them. Thus, when an amino acids are phosphorylated, certain cellular processes can be turned on / off.
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15
Q

What is disulfide bond? What is the significance?

A

It occurs between 2 cysteine residues to form (-S-S-) bonds.

Disulfide bonds can link 2 or more polypeptide chains together covalently, which affects primary structure and thus subsequently affecting other structures (secondary, tertiary…)

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16
Q

What are the names of the 9 essential amino acids?

A

MVP ITT HiLL

Methionine
Valine
Phenylalanine !!!

Isoleucine
Tryptophan
Threonine !!!

Histidine
Leucine
Lysine

17
Q

Which amino acid is most commonly hydroxylated in human body?

A

Proline