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A level Biology > Biological Molecules- Topic 1 > Flashcards

Biological Molecules- Topic 1 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Biomolecule

A

any molecule that is present in living organisms

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2
Q

monomer

A

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

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3
Q

Polymers

A

molecules made from a large
number of monomers joined together.

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4
Q

Condensation reaction

A

bond formed and water released

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5
Q

Hydrolysis reaction

A

bond broken requiring water

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6
Q

maltose

A

2 alpha glucose

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7
Q

sucrose

A

glucose and fructose

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8
Q

polysaccharide

A

the linkage of two or
more monosaccharides by glycosidic bonds.

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9
Q

lactose

A

glucose and galactose

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10
Q

starch

A

glucose polysaccharide

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11
Q

monosaccharide

A

carbohydrate monomer

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12
Q

galactose

A

glucose with OH and H flipped on carbon 4

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13
Q

Fructose

A

5 carbon sugar

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14
Q

Alpha glucose

A

H up on carbon 1

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15
Q

Beta glucose

A

H down on carbon 1

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16
Q

bond between monosaccharides

A

Glycosidic

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17
Q

Starch features

A

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

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18
Q

Starch function

A

The storage carbohydrate of glucose in plants

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19
Q

Starch test

A

Iodine, positive result is blue black colour

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20
Q

Glycogen

A

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

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21
Q

Glycogen features

A

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

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22
Q

Glycogen function

A

Storage molecule of glucose in animals

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23
Q

Cellulose structure

A

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

24
Q

Cellulose function

A

used to make plant cell walls

25
Q

lipid uses

A

membranes, energy source, waterproofing, protection

26
Q

sebum

A

lipid used to waterproof fur and feathers

27
Q

lipids solubility

A

insoluble in water, soluble in organic solvents eg: alcohols

28
Q

Triglyceride

A

Glycerol and 3 fatty acids

29
Q

bond between glycerol and fatty acid/ Phosphate

A

Ester bond

30
Q

Unsaturated fatty acid

A

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

31
Q

Saturated fatty acid

A

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

32
Q

Phospholipid

A

Glycerol, 2 fatty acids and a phosphate molecule

33
Q

Which part of the phospholipid is hydrophillic

A

Phosphate head

34
Q

Which part of the phospholipid is hydrophobic

A

fatty acid tails

35
Q

Saturated acid usual state

A

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

36
Q

Unsaturated acid usual state

A

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

37
Q

protein monomer

A

amino acid

38
Q

Amino acid structure

A

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

39
Q

how many types of amino acids are there

A

20

40
Q

bond between proteins

A

peptide

41
Q

Primary structure of proteins

A

sequence of amino acids

42
Q

secondary structure of proteins

A

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

43
Q

Tertiary structure of proteins

A

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

44
Q

Tertiary structure bonds and interactions.

A

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

45
Q

Globular proteins

A

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

46
Q

Quaternary structure of proteins

A

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

47
Q

Fibrous proteins

A

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

48
Q

denatured

A

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

49
Q

Induced fit model

A

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

50
Q

lock and key model

A

Active site is already completely complementary to substrate

51
Q

Induced fit steps

A

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.

52
Q

Competitive inhibitor

A

Binds to enzymes active site as complementary shape

53
Q

Can competitive inhibitor be overcome

A

Yes, by adding more substrate

54
Q

Non competitive inhibitor

A

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

55
Q

Can non-competitive inhibitor be overcome

A

No

A level Biology (8 decks)

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