Biological Molecules- Topic 1

Question 1

Biomolecule

Answer 1

any molecule that is present in living organisms

Question 2

monomer

Answer 2

single small molecules;
‘building blocks’ from which larger
molecules are made.

Question 3

Polymers

Answer 3

molecules made from a large
number of monomers joined together.

Question 4

Condensation reaction

Answer 4

bond formed and water released

Question 5

Hydrolysis reaction

Answer 5

bond broken requiring water

Question 6

maltose

Answer 6

2 alpha glucose

Question 7

sucrose

Answer 7

glucose and fructose

Question 8

polysaccharide

Answer 8

the linkage of two or
more monosaccharides by glycosidic bonds.

Question 9

lactose

Answer 9

glucose and galactose

Question 10

starch

Answer 10

glucose polysaccharide

Question 11

monosaccharide

Answer 11

carbohydrate monomer

Question 12

galactose

Answer 12

glucose with OH and H flipped on carbon 4

Question 13

Fructose

Answer 13

5 carbon sugar

Question 14

Alpha glucose

Answer 14

H up on carbon 1

Question 15

Beta glucose

Answer 15

H down on carbon 1

Question 16

bond between monosaccharides

Answer 16

Glycosidic

Question 17

Starch features

Answer 17

can be branched or unbranched, chain makes a helix so is compact, insoluble so doesn’t affect water potential

Question 18

Starch function

Answer 18

The storage carbohydrate of glucose in plants

Question 19

Starch test

Answer 19

Iodine, positive result is blue black colour

Question 20

Glycogen

Answer 20

alpha glucose joined at C 1 and 4 and C 1 and 6

Question 21

Glycogen features

Answer 21

Highly branched, insoluble so doesn’t affect water potential, smaller molecules than starch so more easily hydrolysed

Question 22

Glycogen function

Answer 22

Storage molecule of glucose in animals

Question 23

Cellulose structure

Answer 23

Beta glucose, alternate molecules rotated 180 degrees, unbranched, h bonds form between chains so very strong

Question 24

Cellulose function

Answer 24

used to make plant cell walls

Question 25

lipid uses

Answer 25

membranes, energy source, waterproofing, protection

Question 26

sebum

Answer 26

lipid used to waterproof fur and feathers

Question 27

lipids solubility

Answer 27

insoluble in water, soluble in organic solvents eg: alcohols

Question 28

Triglyceride

Answer 28

Glycerol and 3 fatty acids

Question 29

bond between glycerol and fatty acid/ Phosphate

Answer 29

Ester bond

Question 30

Unsaturated fatty acid

Answer 30

1 or more C double bonds are present so molecule is not fully saturated with hydrogen

Question 31

Saturated fatty acid

Answer 31

no C double bonds present so molecule is fully saturated with hydrogen

Question 32

Phospholipid

Answer 32

Glycerol, 2 fatty acids and a phosphate molecule

Question 33

Which part of the phospholipid is hydrophillic

Answer 33

Phosphate head

Question 34

Which part of the phospholipid is hydrophobic

Answer 34

fatty acid tails

Question 35

Saturated acid usual state

Answer 35

Solid, eg: butter as can be packed together tightly due to no bends from double bonds

Question 36

Unsaturated acid usual state

Answer 36

Liquid, eg: oil as they cant pack together closely due to bends from double bonds

Question 37

protein monomer

Answer 37

amino acid

Question 38

Amino acid structure

Answer 38

joined to a central C- NH2 (amino group), R group, H, COOH (carboxylic acid group)

Question 39

how many types of amino acids are there

Answer 39

20

Question 40

bond between proteins

Answer 40

peptide

Question 41

Primary structure of proteins

Answer 41

sequence of amino acids

Question 42

secondary structure of proteins

Answer 42

Hydrogen bonds between amino acids cause peptide chain to form alpha helix or beta pleated sheet

Question 43

Tertiary structure of proteins

Answer 43

Interactions and bonds between R groups of amino acids. Complex 3D shape formed.

Question 44

Tertiary structure bonds and interactions.

Answer 44

Hydrogen bonds, Ionic bonds, disulphide bridges (between to sulphurs), hydrophobic/hydrophillic interactions (weak forces of interaction between non polar groups (van der waals)).

Question 45

Globular proteins

Answer 45

Spherical quaternary proteins with hydrophillic groups on the outside and hydrophobic groups on the inside

Question 46

Quaternary structure of proteins

Answer 46

more than one polypeptide chain held together in a complex 3D structure or the addition of a prosphetic group eg: metal

Question 47

Fibrous proteins

Answer 47

parallel polypeptide chains held together by cross links, usually insoluble eg: collagen

Question 48

denatured

Answer 48

When bonds maintaining a proteins shape are broken eg: by temperature or pH

Question 49

Induced fit model

Answer 49

Enzymes active site slightly changes shape to be completely complementary to substrate

Question 50

lock and key model

Answer 50

Active site is already completely complementary to substrate

Question 51

Induced fit steps

Answer 51

1- When the substrate binds, which can be either at the active site or somewhere else on the enzyme, the active site changes shape. 2-The strain put on the substrate causes it to distort the shape of particular bonds. The activation energy is lowered.

Question 52

Competitive inhibitor

Answer 52

Binds to enzymes active site as complementary shape

Question 53

Can competitive inhibitor be overcome

Answer 53

Yes, by adding more substrate

Question 54

Non competitive inhibitor

Answer 54

Binds to allosteric site, altering the shape of the active site so enzyme substrate complexs can't be formed

Question 55

Can non-competitive inhibitor be overcome

Answer 55

No