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AS biology > biological molecules > Flashcards

biological molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

what are monomers

A

smaller units which can create larger molecules

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2
Q

what are polymers

A

molecules made from lots of monomers joined together

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3
Q

examples of monomers and what polymers they create

A

glucose- starch, glycogen, cellulose
amino acid- proteins
nucleotide- DNA, RNA

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4
Q

what is a condensation reaction

A

joins two molecules together with the formation of a chemical bond and involves the elimination of a water molecule

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5
Q

what is a hydrolysis reaction

A

breaks a chemical bond between two molecules and involves the use of a water molecule

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6
Q

what are monosaccharides

A

the monomers from which larger carbohydrates are made

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7
Q

what are the examples of monosaccharides

A

glucose, fructose, galactose

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8
Q

what monosaccharides have two isomers

A

glucose- alpha glucose and beta glucose

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9
Q

what are isomers

A

same molecular formula but different structures

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10
Q

how are disaccharides formed

A

by the condensation of two monosaccharides

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11
Q

what are the examples of disaccharides

A

maltose, sucrose, lactose

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12
Q

how is maltose formed

A

condensation of two glucose molecules

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13
Q

how is sucrose formed

A

condensation of a glucose molecule and a fructose molecule

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14
Q

how is lactose formed

A

condensation of a glucose molecule and a galactose molecule

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15
Q

how are polysaccharides formed

A

condensation of many glucose monomers

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16
Q

what are the examples of polysaccharides

A

glycogen, starch and cellulose

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17
Q

how is starch formed and what are the bonds between the monomers

A

condensation of alpha glucose monomers
*1-4 glycosidic bonds in amylose
*1-4 and 1-6 glycosidic bonds in amylopectin

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18
Q

what is the function of starch and where is it located

A

store of glucose, located in plant cells e.g. within the chloroplast

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19
Q

what is the structure of starch

A

made of 2 polymers:
-amylose, an unbranched helix
-amylopectin, branched molecule

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20
Q

explain how the structure of the starch leads to its function

A

helix can compact to fit a lot of glucose in a small space. BRANCHED STRUCTURE increases surface area for rapid hydrolysis back to glucose. insoluble so wont affect water potential

21
Q

how is cellulose formed and what are the bonds between the monomers

A

formed by the condensation of beta-glucose monomers
*1-4 glycosidic bonds

22
Q

what is the function of cellulose and where is it located

A

cellulose provides structural strength for the cell wall in plants

23
Q

what is the structure of starch

A

polymer forms long straight chains, chains are held in parallels by many hydrogen bonds to form fibrils

24
Q

explain how the structure of cellulose leads to its function

A

many hydrogen bonds provide collective strength. also insoluble so wont affect water potential

25
Q

how is glycogen formed and what are the bonds between monomers

A

formed by the condensation of alpha glucose monomers
*1-4 and 1-6 glycosidic bonds

26
Q

what is the function of glycogen and where is it located

A

glycogen is used as a store of glucose. glycogen is found in animals, mainly in muscle and liver cells

27
Q

what is the structure of glycogen

A

highly branched molecule

28
Q

explain how the structure of glycogen is related to its function

A

branched structure increases surface area for rapid hydrolysis back to glucose. insoluble so wont affect water potential

29
Q

how are triglycerides formed

A

by the condensation of one molecule of glycerol and three molecules of fatty acids

30
Q

how are ester bonds formed

A

by a condensation reaction between glycerol and a fatty acid (RCOOH)

31
Q

what can the R group of a fatty acid be

A

saturated or unsaturated

32
Q

what is a saturated fatty acid

A

when the hydrocarbon chain has no double bonds between carbons

33
Q

what is an unsaturated fatty acid

A

when the hydrocarbon chain has one or more double bonds between carbons

34
Q

what are the properties of triglycerides

A

1.energy storage- due to the large ratio of energy storing carbon hydrogen bonds compared to the number of carbon atoms, a lot of energy is stored in the molecule
2.metabolic water source- due to high ratio of hydrogen or oxygen atoms, triglycerides can release water when oxidised, essential of animals in the desert
3.do not affect water potential, large and hydrophobic, making them insoluble in water

35
Q

what are the functions of triglycerides

A

1.insulation
2.buoyancy
3.protection

36
Q

what are phospholipids made up of

A

2 fatty acids, glycerol molecule and a phosphate group

37
Q

what are the properties of phospholipids

A
  1. hydrophillic ‘head’. due to negative charge on phosphate group it attracts water and repels fats as it is charged
  2. hydrophobic ‘tail’ fatty acid chain is not charged, so repels water but will mix with fats
  3. phospholipids can form bilayers as there are two charged regions, in water they are positioned so that the heads are exposed to the water and the tails are not. forms a phospholipid bilayer membrane structure which makes up the plasma membrane around cells
38
Q

describe how amino acids join together

A

through a condensation reaction, which removes a water molecule between the carboxyl group of one and the amine group of another, forming a peptide bond

39
Q

how are dipeptides formed

A

condensation reaction between two amino acids

40
Q

how are polypeptides formed

A

condensation reaction between many amino acids

41
Q

what is the primary structure of a protein

A

the sequence of the amino acids in the polypeptide chain

42
Q

what is the secondary structure of a protein

A

the sequence of amino acids causes parts of a protein molecule to bend into alpha-helix shapes or fold into beta-pleated sheets. hydrogen bonds hold the secondary structure

43
Q

what is the tertairy structure of a protein

A

the further folding of the secondary structure to form a unique 3D shape, held in place by ionic, hydrogen and disulphide bonds

44
Q

why is the 3D shape of a tertiary structure important

A

makes each protein distinctive and allows it to recognise and be recognised by other molecules

45
Q

what is the quaternary structure of a protein

A

the combination of a number of different polypeptide chains
-e.g. iron-containing haem group in haemoglobin

46
Q

test for proteins

A

biuret test- detects peptide bond
1. place a sample of the solution to be tested in a test tube and add an equal volume of sodium hydroxide solution at room temp
2. add a few drops of very dilute copper sulfate solution and mix gently
3. a purple coloration indicates the prescence of peptide bonds and hence a protein

47
Q

fibrous proteins

A

e.g. collagen
-structural functions

48
Q

gobular proteins

A

e.g. haemoglobin and enzymes
-carry out metabloc functions

49
Q
A

AS biology (7 decks)

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