Proteins 2 Flashcards

1
Q

Essential amino acids

A

(9) cannot be produced naturally, must be consumed through our diet

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2
Q

Non-essential amino acids

A

(11) synthesised from products or intermediates of crucial metabolic pathways

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3
Q

What is alanine synthesised from?

A

pyruvate, a product of glycolysis

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4
Q

What is aspartate synthesised from?

A

oxaloacetate, an intermediate of the citric acid cycle

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5
Q

How can amino acids be classfied?

A

Based on their metabolic fate:

  • glucogenic
  • ketogenic
  • both

Based on their R-group which determines the amino acids properties/characteristics such as solubility in water

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6
Q

What proteinogenic amino acids?

A

‘protein creating’ –> there are 22 genetically encoded amino acids in known life:

  • 20 standard amino acids
  • 2 additional which are incorporated by special transformational mechanisms
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7
Q

define non standard amino acids

A

refers to amino acids that have been chemically modified after they have been incorporated into a protein

have biologically important roles

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8
Q

define standard amino acids

A

non-proteinogenic, not naturally encoded amino acids

example = pyrrolysine- has broad potential in biotech

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9
Q

classification of amino acids on the basis of their R-groups

A
non-polar - hydrophobic
polar, hydrophilic - but uncharged
basic - +ve charged
acidic - -ve charged
aromatic - relatively non-polar, participates in hydrophobic interactions
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10
Q

how can amino acids be visualised?

A

ball and stick model

space filling model

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11
Q

amino acids with non polar R-groups

A
glycine
alanine
valine
leucine
methionine
isoleucine
proline
phenylalanine
tryptophan
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12
Q

amino acids with polar R groups

A
serine
threonine
asparagine
glutamine
cysteine
tyrosine
aspartic acid
glutamic acid
histidine
lysine
arginine
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13
Q

basic amino acids

A

lysine
arginine
histidine

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14
Q

acidic amino acids

A

asparagine/aspartic acid

glutamine/glutamic acid

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15
Q

aromatic amino acids

A

phenylalanine
tyrosine
tryphophan

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16
Q

features of globular proteins

A

compact, soluble, spherical

17
Q

features of fibrous proteins

A

elongated and insoluble

18
Q

Most living systems are based on which enantiomer of alpha amino acids

A

L form- only L amino acids are constituent of proteins.

S absolute configuration (with the exception of cysteine)

19
Q

define pK

A

the logarithmic value of the dissociation constant, Ka, of a hydrogen atom present on a molecule

20
Q

Zwitterionic form

A

At neutral pH, the carboxyl group of an amino acid is deprotonated and the amino group is protonated –> the net charge is zero

The amino acid can act as an acid or a base and is said to be amphoteric

21
Q

Types of amino acid configuration

A
  • Operational classification
  • Fischer convention
  • Cahn Ingold Prelog
22
Q

Operational Classification

A

Amino acids classified depending on whether they rotate the plane of polarise light clockwise ot counter clockwise from the point of view of the observer

23
Q

Fischer convention

A

Configuration based on glyceraldehyde.
Have to look down the alpha carbon- hydrogen bond with the hydrogen hid behind the plane of view

CORN anticlockwise = L
CORN clockwise = D

The amino acid must be orientated so that the carbon chain is vertical and the carboxyl group is on the top.

The amino acid is projected onto a flat screen:
L isomer - if the amino group is on the left of the chiral carbon
D isomer - if the amino group is on the right of the chiral carbon

24
Q

Cahn Ingold Prelog System

A

The 4 groups surrounding a chiral centre are ranked according to a priority scheme.

CORN anticlockwise, lowest –> highest Ar = S isomer
CORN clockwise, lowest –> highest Ar = R isomer