Unit 1 - Biological Molecules Flashcards

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1
Q

Monomer (1)

A
  • The smaller units from which larger
    molecules are made
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2
Q

Polymer (1)

A
  • Molecules made from a large
    number of monomers joined
    together
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3
Q

Monosaccharide (1)

A
  • The monomers from which larger
    carbohydrates are made
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4
Q

Disaccharide (2)

A
  • Formed by the condensation of two
    monosaccharides
  • held together by a glycosidic bond
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5
Q

Polysaccharide (2)

A
  • Formed by the condensation of
    many glucose units
  • held by glycosidic bonds
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6
Q

Cellulose (2)

A
  • Polysaccharide in plant cell walls
  • formed by the condensation of
    β-glucose
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7
Q

Glycogen (2)

A
  • Polysaccharide in animals
  • formed by the condensation of
    α-glucose
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8
Q

Starch (3)

A
  • Polysaccharide in plants
  • formed by the condensation of
    α-glucose
  • contains two polymers - amylose
    and amylopectin
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9
Q

Glycosidic bond (4)

A
  • C–O–C link
  • between two sugar molecules
  • formed by a condensation reaction
  • it is a covalent bond
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10
Q

Amylose (4)

A
  • Polysaccharide in starch
  • made of α-glucose
  • joined by 1,4-glycosidic bonds
  • coils to form a helix
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11
Q

Amylopectin (4)

A
  • Polysaccharide in starch
  • made of α-glucose
  • joined by 1,4 and 1,6-glycosidic
    bonds
  • branched structure
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12
Q

Condensation
reaction (3)

A
  • A reaction that joins two molecules
    together
  • with the formation of a chemical
    bond
  • involves the elimination of a
    molecule of water
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13
Q

Hydrolysis
reaction (3)

A
  • A reaction that breaks a chemical
    bond
  • between two molecules
  • involves the use of a water molecule
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14
Q

Fibrils (2)

A
  • Long, straight chains of β-glucose
    glucose
  • held together by many hydrogen
    bonds
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15
Q

Triglyceride (2)

A
  • Formed by the condensation of 1
    molecule of glycerol and 3
    molecules of fatty acids
  • forming 3 ester bonds
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16
Q

Phospholipid (3)

A
  • Formed by the condensation of one
    molecule of glycerol and two
    molecules of fatty acid
  • held by two ester bonds
  • a phosphate group is attached to
    the glycerol
17
Q

Induced-fit
model (4)

A
  • The enzyme active site is not
    initially complementary to the
    substrate
  • the active site moulds around the
    substrate
  • this puts tension on bonds
    lowers the activation energy
18
Q

Competitive
inhibitor (3)

A
  • A molecule that is the same/similar
    shape as the substrate
  • binds to the active site
  • prevents enzyme-substrate
    complexes from forming
19
Q

Non-competitive
inhibitor (3)

A
  • A molecule that binds to an enzyme
    at the allosteric site
  • causing the active site to change
    shape
  • preventing enzyme-substrate
    complexes from forming
20
Q

Primary
structure (1)

A
  • The sequence of amino acids on a
    polypeptide chain
21
Q

Secondary structure (3)

A
  • The folding or coiling
  • to create a β pleated sheet or an
    α helix
  • held in place by hydrogen bonds
22
Q

Tertiary structure (3)

A
  • The further folding
  • to create a unique 3D shape
  • held in place by hydrogen, ionic and
    sometimes disulphide bonds
23
Q

Quaternary
structure (1)

A
  • More than one polypeptide chain in
    a protein
24
Q

Peptide bond (3)

A
  • Covalent bond joining amino acids
    together in proteins
  • C–N link between two amino acid
    molecules
  • formed by a condensation reaction
25
Q

What is the effect of
temperature on enzyme-controlled reaction? (4)

A
  • Low temp: not enough kinetic energy for successful collisions between the
    enzyme and substrate.
  • Too high temp: enzymes denature
  • the active site changes shape
  • enzyme- substrate complexes cannot
    form.