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Biology > 1 - Biological Molecules > Flashcards

1 - Biological Molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Monomer

A

one of many small molecules that joins together to make a large one (polymer)

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2
Q

Polymer

A

a large molecule made up of small repeating units called monomers

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3
Q

Monosaccharide

A

sweet tasting, soluble, single sugar molecules

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4
Q

General formula of monosaccharides

A

(CH2O)n

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5
Q

Condensation

A

joining together of two units/molecules to form a larger one with the elimination of a water molecule

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6
Q

Hydrolysis

A

breaking apart of two units/molecules to form monomers requiring a molecule of water

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7
Q

Carbohydrates

A

carbon and water molecules

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8
Q

Carbon’s special properties

A

can form 4 covalent bonds and bond with itself to form a ‘backbone’ in organic compounds

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9
Q

Glucose

A

monosaccharide, a hexose (6 carbon sugar), two possible isomers/arrangements

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10
Q

Alpha glucose structure and formula

A

C6H12O6, OH bonded at the bottom

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11
Q

Beta glucose structure and formula

A

C6H12O6, OH bonded at top on right side

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12
Q

Reducing sugar (all mono and some disaccharides)

A

a sugar that is able to donate an electron to another chemical

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13
Q

Reduction

A

a chemical reaction that involves the gain of electrons or hydrogen

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14
Q

Benedict’s reagent

A

an alkaline solution of copper II sulfate, when heated with a reducing sugar it forms an insoluble red precipitate of copper oxide

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15
Q

Method to test for reducing sugars

A

add equal volume of (liquid) sample to Benedict’s reagent, heat in a water bath for 5 minutes

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16
Q

Disaccharides

A

monosaccharides bonded in pairs

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17
Q

Maltose

A

glucose + glucose

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18
Q

Sucrose

A

fructose + glucose

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19
Q

Galactose

A

lactose + glucose

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20
Q

Monosaccharide bonding

A

a condensation reaction occurs and a glycosidic bond is formed, a molecule of water is released

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21
Q

Disaccharides splitting/breaking apart

A

a hydrolysis reaction occurs and a glycosidic bond is broken, a molecule of water is required

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22
Q

Non-reducing sugars

A

sugars that cannot donate an electron to another chemical (eg. sucrose), must be hydrolysed to see if it is non-reducing

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23
Q

Test for non-reducing sugars

A

Benedict’s test as normal, if a reducing sugar is not shown to be present add equal volume of fresh sample to HCl. Heat in a water bath for 5 mins (hydrolysis). Slowly add NaHCO3 to neutralize. Test pH to check alkalinity. Retest with Benedict’s reagent, if goes orange/brown, non-reducing sugar present in initial sample

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24
Q

Polysaccharide

A

many monosaccharides bonded with glycosidic bonds from condensation reactions

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25
Q

Polysaccharide properties

A

Insoluble so good for storage, when hydrolysed form monos. and disacc.
Some are used for structural support in plants (cellulose)

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26
Q

Starch

A

200-100000 alpha glucose molecules bonded together by glycosidic bonds, can be branched or unbranched

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27
Q

Starch; where it is found

A

found as granules/grains in plants, in seeds and storage organs

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28
Q

Starch; role

A

main role is energy storage, important component in foods as it is main energy source

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29
Q

Starch; structure

A

Insoluble so doesn’t affect water potential or diffuse out of cells, hydrolysed into alpha glucose monomers for respiration, wound into tight coils so compact (large amounts of energy can be stored in a small space)

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30
Q

Glycogen

A

found in animals but not plants, main carb storage, shorter and more highly branched than starch, stored as granules in liver and muscles

31
Q

Glycogen; suitable for storage

A

Insoluble so doesn’t affect water potential (osmosis), doesn’t diffuse out of cells, compact so large amounts of energy stored in small space

32
Q

Glycogen; short and highly branched

A

quicker to be worked at by enzymes to produce glucose for respiration

33
Q

Cellulose

A

straight, unbranched, parallel chains of beta glucose, chains grouped together in microfibrils (arranged in fibres)

34
Q

Cellulose; cross linkages

A

hydrogen bonds form cross links that overall add to its strength making it a valuable structural material

35
Q

Cellulose; uses

A

cell wall - gives cells rigidity and stops them bursting due to too much water entering by osmosis
Important for stems and leaves to maintain max. SA

36
Q

Cellulose; rotation

A

alternate molecules rotated 180 degrees so -OH groups are next to each other to form glycosidic bonds

37
Q

Triglycerides

A

formed by the condensation of one molecule of glycerol and three molecules of fatty acid to form ester bonds

38
Q

Triglycerides; source of energy

A

high ratio of energy storing carbon-hydrogen bonds to carbon atoms so excellent source of energy

39
Q

Triglycerides; low mass to energy ratio

A

store lots of energy in a small volume, beneficial to animals as it reduces volume of mass they have to carry around

40
Q

Triglycerides; non-polar molecules

A

large, non-polar and so insoluble in water - doesn’t affect water potential in cells

41
Q

Triglycerides; ratio of hydrogen to oxygen

A

high ratio of hydrogen to oxygen atoms, so releases water when oxidised - important source of water in desert animals

42
Q

Triglycerides; differences in properties

A

differences in properties of triglycerides is due to differences in the structures of the fatty acids they contain

43
Q

Fatty acids

A

represented by RCOOH, R represents a saturated or unsaturated backbone, all have the functional group -COOH (carboxyl group)

44
Q

Fatty acids; saturation

A

can be saturated, monounsaturated or polyunsaturated

45
Q

Saturated

A

no double bonds between CARBON atoms

46
Q

Monounsaturated

A

one double bond between CARBON atoms

47
Q

Polyunsaturated

A

more than one double bond between CARBON atoms

48
Q

Phospholipids

A

lipid containing a phosphate group, consists of a molecule of glycerol, 2 molecules of fatty acid and one phosphate molecule

49
Q

Phospholipids; properties

A

hydrophilic head (phosphate) and hydrophobic tail (fatty acids), makes them polar molecules as they have two poles/ends that behave differently with water

50
Q

Phospholipids; bilayers

A

in aqueous environments they form a phospholipid bilayer (eg. within cell membranes) causing a hydrophobic barrier to be formed between the inside and outside of a cell

51
Q

Phospholipids; glycolipids

A

phospholipid structure allows them to combine with carbohydrates to form glycoproteins within the cell membrane, these are important in cell recognition

52
Q

Glycerol

A

each of the three OH hydroxyl groups can form an ester bond (C-O-C) with a fatty acid or phosphate group

53
Q

Phosphate group

A

RPO2(OH)2 - hydrophilic groups that form an ester bond when they bond to glycerol

54
Q

Amino acids

A

monomer units of polypeptide chains, which make up proteins

have a central carbon atom with a amine group, carboxyl group, R group, and hydrogen attached

55
Q

Peptide bonds

A

bonds that form between amino acids in condensation reactions (between carboxyl group and amine group)

56
Q

Primary structure of proteins

A

sequence of amino acids in polypeptide chain

decides its ultimate shape and hence function

57
Q

Secondary structure of proteins

A

H bonds between -NH group at one location and -C=O group at another location
causes polypeptide chain to be held in a folded shape eg. helix

58
Q

Tertiary structure of proteins

A

secondary structure (helix) can often be twisted and coiled further by ionic bonds and disulfide bridges to give a more complex shape

59
Q

Disulfide bridges in proteins

A

single covalent bond between two sulphur atoms of different amino acids, strong and not easily broken

60
Q

Ionic bonds in proteins

A

form between any carboxyl and amino groups that are not involved in forming peptide bonds
weaker than disulfide bridges
easily broken by changes in pH

61
Q

Quaternary structure of proteins

A

structure formed by presence of many polypeptide chains linked together
may include non-proteins (prosthetic) components eg. haem group

62
Q

Biuret test for proteins

A

add sample to test tube
add equal volume of sodium hydroxide solution
add few drops of very dilute copper II sulphate solution
purple colour indicates presence of peptide bonds and hence proteins

alternatively, add Biuret solution to sample for same observations

63
Q

Enzymes

A

globular proteins that act as biological catalysts by lowering the activation energy of reactions (allows metabolic processes to occur at internal body temperature

64
Q

Catalysts

A

alter the rate of chemical reaction without undergoing permanent changes themselves (can be reused and so are effective in small amounts)

65
Q

For reactions to occur naturally:

A

reactant molecules must collide with SUFFICIENT ENERGY to alter the arrangement of atoms
the free energy of the reactant must be more than that of the products
activation energy must be supplied

66
Q

Functional region of enzyme…

A

active site

67
Q

Induced fit model

A

active site forms as the enzyme and substrate interact, enzymes can change the shape of their active site so that it is complementary to the substrate

as it changes shape, strain is put on the substrate molecule, distorting bonds in the substrate and lowering the activation energy

68
Q

Substrate and enzyme have shapes that are

A

complementary (not the same but have ability to fit together)

69
Q

Enzyme + substrate =

A

enzyme-substrate complex

70
Q

Lock and key theory

A

a substrate will only fit the active site of a particular enzyme
(suggests enzymes have a rigid structure)

71
Q

Competitive inhibitors

A

have a molecular shape similar to that of the substrate and is also complementary to the active site of the enzyme
able to occupy enzymes active site and prevent formation of enzyme-substrate complexes

72
Q

Substrate concentration increased, effect of COMPETITIVE inhibitor…

A

reduced

73
Q

Non-competitive inhibitors

A

bind to the enzyme at a site other than the active site, this alters the shape of the enzyme and hence the shape of the active site
prevents formation of enzyme-substrate complex

74
Q

Substrate concentration increased, effect of NON-COMPETITIVE inhibitor…

A

not changed - the substrate and non-competitive inhibitor are not competing for the same site

Biology (21 decks)

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