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module 2: foundations to biology > 2.2 biological molecules > Flashcards

2.2 biological molecules Flashcards

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1
Q

what is a monomer

A

a single unit/molecule that binds to other identical monomers to form a polymer

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2
Q

what is a polymer

A

a large molecule mad up of many monomers joined together

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3
Q

what is a dimer

A

two monomers joined together

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4
Q

what is a covalent bond and what is it between

A

sharing electrons with other atoms
two non metals

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5
Q

what is a hydrogen bond

A

a weak interaction that occurs when two molecules contain a slightly + charged and - charged hydrogen atom

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6
Q

what is a condensation reaction

A

two molecules joined with the removal of water

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7
Q

what is a hydrolysis reaction

A

molecule split into two smaller molecules with the addition of water

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8
Q

name the properties of water

A

liquid
ice is less dense
solvent
strong cohesion and surface tension properties
high specific heat capacity
high latent heat of vapourisation
reactant

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9
Q

describe what is meant by water being a liquid

A

its constantly moving around and is making and breaking hydrogen bonds

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10
Q

what are the benefits of water being at liquid at room temperature

A

provides habitats
forms a major component of living tissues
provides a reaction medium
provides a transport medium

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11
Q

describe what happens to water as it reaches about 4 degrees and freezes

A

as water gets cooler it gets more dense until 4 degrees
the polar nature means the water molecules realign themselves in a less dense structure
the hydrogen bonds hold the molecules further apart
so the layer floats

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12
Q

why is it beneficial that ice is less dense then water

A

provides an insulating layer and helps keep a stable environment
so aquatic animals can still swim etc.

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13
Q

why is water a solvent and what does it allow

A

its polar so its attracted to the + and - solutes
allows molecules/ions to be transported (dissolved) and move around and react together

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14
Q

what does cohesion and surface tension mean and allow

A

hydrogen bonds pull the water molecules closer together
at the surface it allows it to contract and resist force applied

water to be pulled up through a column and insects to walk on it

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15
Q

why does water have a high specific heat capacity and what does it provide

A

it can absorb a lot of energy and doesn’t heat up or cool down quickly
provides a stable environment to live in and a stable temp for enzymes

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16
Q

what does high latent heat of vapourisation mean and what does it do

A

a large amount of energy to be absorb to evaporate
keeps temp stable
cools living things

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17
Q

name the inorganic cations and their symbol form

A

calcium Ca*2+
Sodium Na+
Potassium K+
Hydrogen H+
Ammonium NH4+

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18
Q

name the inorganic anions

A

nitrate NO3-
Hydrogencarbonate HCO3-
Chloride Cl-
Phosphate PO4 *3-
Hydroxide OH-

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19
Q

what is a deficiency

A

not consuming enough of a particular ion

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20
Q

what are amino acids and their structure

A

monomers of all proteins
central carbon
carboxyl group (COOH)
amino group (NH2)
R group
hydrogen

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21
Q

what is a protein and name their functions

A

large polymers of amino acids
-structural components
-adopt specific shapes
-membranes have protein constitutes that act as carriers/ pores for active transport/f.diffusion

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22
Q

what is the bond formed between amino acids

A

peptide bonds

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23
Q

what is a dipeptide

A

two amino acids joined together

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24
Q

what is a polypeptide

A

a long chain of amino acids joining together

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25
Q

what reactions creates a peptide bond between two amino acids

A

condensation reaction
produces water a product
(-COOH) from one amino acid becomes (-CO)
(-NH2) from the other aa becomes (-NH) with a peptide bond between them
the OHH makes water (H20)

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26
Q

what reactions breaks the peptide bond between two amino acids

A

hydrolysis
addition of water and is used up

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27
Q

what is the primary structure of a protein

A

sequence of amino acid in a protein chain (polypeptide)

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28
Q

why is it important that the order of amino acids doesn’t change in the primary structure

A

order determines the structure and shape of the protein and therefore the function

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29
Q

what is the secondary structure of an amino acid

A

chain of amino acid coils into an alpha helix or folds into a beta pleated sheet

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30
Q

what bond is in the secondary structure and what is it between

A

hydrogen bonds between the amino and carboxyl group of different amino acids
3D

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31
Q

what is the tertiary structure of a protein

A

overall 3D shape of a protein
coils and pleats begin to fold in with areas of straight chains

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32
Q

what bonds hold the tertiary structure and in what shape

A

hydrogen, disulfide and ionic bonds between R groups
very precise shape
-globular proteins or fibrous proteins

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33
Q

what is the quaternary structure of a protein

A

more then one polypeptide chain and a non protein group

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34
Q

what bonds hold a quaternary structure

A

hydrogen, disulfide and ionic bonds

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35
Q

what do hydrogen bonds form between

A

form between hydrogen atoms with slight positive charge and other atoms with a slight negative charge

36
Q

what groups in amino acids do hydrogen bonds form between

A

amino, carboxyl, hydroxyl groups

37
Q

what is the role of hydrogen bonds

A

keeps tertiary and quaternary structure of protein in the correct shape
provides strength

38
Q

what do ionic bonds form between

A

carboxyl and amino groups part of the R group

39
Q

what do ionic bonds do to the groups

A

ionises them into NH3+ and COO-
strong attraction which forms bond

40
Q

what do disulfide bonds form between and what type of bond is it

A

between the R groups of two cysteines containing sulfur
strong covalent bond

41
Q

what do hydrophobic parts of R groups do

A

associate in the center of the polypeptide to avoid water

42
Q

what do hydrophilic parts of R groups do

A

associate near the edge of the polypeptide to be close to water

43
Q

what do hydrophobic and hydrophilic interactions cause

A

twisting of amino acid chain
results in protein changing shape

44
Q

what are globular proteins

A

spherically shaped molecules which are soluble in water and have metabolic roles within an organism

45
Q

how are globular proteins water soluble

A

has hydrophobic R groups turned inwards
hydrophillic R groups on the outside
so water molecules easily cluster around them and bind to them

46
Q

what are fibrous proteins

A

a long, thin structure thats insoluble in water, metabolically inactive but provides structural roles within an organism

47
Q

name 3 fibrous proteins

A

collagen
keratin
elastin

48
Q

name 3 globular proteins

A

haemoglobin
insulin
pepsin

49
Q

what is the function of collagen and name some specific examples

A

provide mechanical strength
-arteries = a layer helps to withstand high pressure
-tendons=connect muscle to bone helps to pull bones
-bones=makes them hard reinforced with calcium phosphate
-cartilage and connective tissue

50
Q

what is the function of keratin and why is it suited to its role

A

provides mechanical strength and protection (strong hard body parts)
nails,hair,claws,hooves,horns etc
contains lots of cysteine (amino a.) so lots of strong disulfide bridges

51
Q

what is the function of elastin and why is it suited to its role

A

allows stretching/ adaption of shape in living things
cross linking and coiling make it strong and extensible
-skin, lungs, blood vessels

52
Q

haemoglobin
-structure
-type of protein?
-function/how it works

A

(quaternary)
made of 4 polypeptide chains (2x alpha globin chains and 2x beta globin chains)
has a haem group / prosthetic group containing iron ion
is a conjugated protein
oxygen binds to each of tthe 4 haem groups

53
Q

what is the structure of insulin

A

made of two polypeptide chains
A chain begins with an alpha helix
B chain ends with a beta pleated sheet
tertiary structure joined by disulfide links

54
Q

how is insulin suited to its role

A

hydrophillic R groups = outside = soluble in water
insulin binds to glycoprotein receptors

55
Q

pepsin
-function
-structure
-how is it suited to conditions

A

digest protein in the stomach
single polypeptide chain, folds into a symmetrical tertiary structure
very few AA with basic R groups, more with acidic R groups , few basic groups to accept H+ ions = stable

56
Q

what is a prosthetic group

A

a non protein group that’s permanently attached to a protein

57
Q

what is a conjugated protein

A

a protein associated with a non protein group

58
Q

what do carbohydrates contain

A

carbon
hydrogen
oxygen

59
Q

what are the role of carbohydrates

A

source of energy
store of energy
structural units

60
Q

what are monosaccharides

A

simplest carbohydrates

61
Q

state the properties of monosaccharides

A

source of energy due to large number of h-C bonds
taste sweet
soluble in water
insoluble in non polar solvents
exists as straight chains/ring/cyclic forms
monomers of complex carbs

62
Q

what are disaccharides and what are they joined by

A

two monosaccharides joined together by glycosidic bonds

63
Q

name properties of disaccharides

A

sweet
soluble

64
Q

name 4 examples of disaccharides and what they are made of

A

alpha glu. + alpha glu. = maltose
beta glu. + fructose = sucrose
beta galactose + alpha glu.= lactose
beta + beta = cellobiose

65
Q

what reactions forms and breaks glycosidic bonds

A

condensation reaction
hydrolysis

66
Q

name a non reducing sugar

A

sucrose

67
Q

name reducing sugars

A

maltose and lactose

68
Q

what is the structural difference between alpha and beta glucose

A

the hydroxyl group and hydrogen on carbon 1 are reversed

69
Q

what is the structural difference between ribose and deoxyribose

A

ribose has two hydoxyl groups on carbon 2/3
deoxy only has it on carbon 3

70
Q

what type of sugar are alpha and beta glucose

A

hexose

71
Q

what type of sugar is ribose and deoxyribose

A

pentose

72
Q

what are polysaccharides

A

polymers of monosaccharides

73
Q

what is homopolysaccharide and heteropolysaccharide

A

homo= same type of monosaccharides
hetero= different types

74
Q

describe the structure of starch and its function

A

alpha glucose
in two different structural units
-amylopectin
-amylose
storage of energy in plants

75
Q

describe the structure of amylose

A

long chain of alpha glucose in coil shape
1-4 glycosidic bonds
hydrogen bonds hold coil
less soluble

76
Q

describe the structure of amylopectin

A

long chain of alpha glucose
1-4 glycosidic bonds
1-6 glycosidic bonds = branched

77
Q

describe the structure of glycogen and function

A

long chain of alpha glucose
1-4 glycosidic bonds
1-6 glycosidic bonds = branched
compact
act as energy store in animals

78
Q

describe the structure of cellulose

A

homopolysaccharide of beta glucose
1-4 beta glycosidic bonds
straight chain
(hydroxyl and hydrgoen)reversed so straight chain

79
Q

what is a phospholipid

A

2 fatty acids and a phosphate head joined to a glycerol backbone

80
Q

how do phospholipids behave in water

A

hydrophobic fatty acid tails are non polar and repel water so face inwards
hydrophillic phosphate head is polar and attracts water so faces outwards

81
Q

what is a bilayer and what does it form

A

two layers of phospholipids
membranes

82
Q

what is cholesterol

A

steroid alcohol/ sterol which is a lipid not made of glycerol or fatty acids
made of 4 carbon based rings

83
Q

what is the role of cholesterol

A

provide stability/ regulate fluidity of membrane

84
Q

what is a triglyceride

A

A glycerol and 3 fatty acids

85
Q

What is the structure of a glycerol

A

3 carbon
Each have one OH
Filled with H

86
Q

Which is more soluble amylose or amylopectin

A

Amylose

module 2: foundations to biology (6 decks)

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