Biological molecules Flashcards

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1
Q

Phospholipid structure

A

-phosphoric acid head (hydrophilic)
-glycerol
-2 fatty acid chains (hydrophobic)

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2
Q

Triglyceride

A

-one glycerol
-3 fatty acid chains
-ester bond (esterification)

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3
Q

Difference between saturated and unsaturated fatty acids

A

Saturated - No carbon-carbon double bond (have kinks)
(Fats)
Unsaturated - carbon-carbon double bond (no kinks)
(Oils)

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4
Q

Amino acid structure

A

Amine group (NH2)
Carboxyl group (COOH)
R-group (variant)
Hydrogen

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5
Q

Polypeptide chain

A

Long chain of two or more amino acids joined together by peptide bonds

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6
Q

Peptide bond

A

Condensation reaction between carboxyl group and hydroxyl group
H2O released

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7
Q

Levels of protein structure

A

Primary - Specific sequence of amino acids in polypeptide
Secondary - Primary but coiled or folded on itself, hydrogen bonds β, α
Tertiary - Further coiled/folded, 3D shape
Quaternary - Interaction between two or more polypeptides

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8
Q

α (secondary) helix

A
  • strong
  • helical shape
  • result of hydrogen bonds
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9
Q

β (secondary) pleated sheet

A
  • weak
  • strength achieved through layers and bonds
  • result of hydrogen bonds
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10
Q

Interactions between R-groups (tertiary)

A

-disulphide bonds
-ionic bonds
-hydrogen bonds
-hydrophilic/hydrophobic reactions

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11
Q

Haemoglobin

A
  • biologically active when it becomes a quaternary structure
  • 4 sub-chain units (2 alpha and 2 beta)
  • has a prosthetic group called haem group (carry pigment and iron)
  • globular protein
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12
Q

Globular proteins

A
  • Roll up to form a ball
  • Hydrophobic R-groups turn inwards so hydrophilic R-groups outwards
  • Usually have metabolic roles
  • Enzymes, Plasma proteins, Antibodies, Hormones (insulin), haemoglobin
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13
Q

Fibrous Proteins

A
  • Form fibers
  • Repetitive sequence of amino acids
  • Usually insoluble
  • Structural roles
  • Collagen and keratin
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14
Q

Difference between collagen (C) and haemoglobin (H)

A
  • H is globular, C is fibrous
  • H is soluble, C is insoluble
  • H has a range of amino acids , C primary structure = 35% glycine
  • H has prosthetic haem group, C has no prosthetic group
  • H has 2 alpha and 2 beta, C is majority left- handed helix structures
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15
Q

Roles of water

A
  • Solvent
  • Liquid
  • Cohesion and adhesion
  • Freezing
  • High latent and thermal stability
  • Metabolic
  • Habitat
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16
Q

Why is a molecule polar?

A

One region of molecule is on average negatively charged than the opposite region
Slightly negative attracted to slightly positive

17
Q

Structure of water

A
  • Oxygen slightly negatively charged
  • Hydrogen slightly positively charged
  • Covalent bonds
18
Q

What are monomers and polymers?

A
  • Monomer : Individual molecules
  • Polymer : The individual molecules bonded to identical molecules
    e.g. chain of identical glucose molecules (monomer) is a (polymer) called starch
19
Q

What is a condensation reaction?

A
  • Two molecules join together
  • Release water
    e.g. two glucose molecules
20
Q

What is an hydrolysis reaction?

A
  • When a water molecule is added to split two molecules