Unit 1 - Biological Molecules Flashcards
1
Q
Monomer (1)
A
- The smaller units from which larger
molecules are made
2
Q
Polymer (1)
A
- Molecules made from a large
number of monomers joined
together
3
Q
Monosaccharide (1)
A
- The monomers from which larger
carbohydrates are made
4
Q
Disaccharide (2)
A
- Formed by the condensation of two
monosaccharides - held together by a glycosidic bond
5
Q
Polysaccharide (2)
A
- Formed by the condensation of
many glucose units - held by glycosidic bonds
6
Q
Cellulose (2)
A
- Polysaccharide in plant cell walls
- formed by the condensation of
β-glucose
7
Q
Glycogen (2)
A
- Polysaccharide in animals
- formed by the condensation of
α-glucose
8
Q
Starch (3)
A
- Polysaccharide in plants
- formed by the condensation of
α-glucose - contains two polymers - amylose
and amylopectin
9
Q
Glycosidic bond (4)
A
- C–O–C link
- between two sugar molecules
- formed by a condensation reaction
- it is a covalent bond
10
Q
Amylose (4)
A
- Polysaccharide in starch
- made of α-glucose
- joined by 1,4-glycosidic bonds
- coils to form a helix
11
Q
Amylopectin (4)
A
- Polysaccharide in starch
- made of α-glucose
- joined by 1,4 and 1,6-glycosidic
bonds - branched structure
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
13
Q
Hydrolysis
reaction (3)
A
- A reaction that breaks a chemical
bond - between two molecules
- involves the use of a water molecule
14
Q
Fibrils (2)
A
- Long, straight chains of β-glucose
glucose - held together by many hydrogen
bonds
15
Q
Triglyceride (2)
A
- Formed by the condensation of 1
molecule of glycerol and 3
molecules of fatty acids - forming 3 ester bonds
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.