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

2.2 biological molecules Flashcards

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 chemical and physical properties of water

A

Chemical
- polar
- hydrogen is delta +, oxygen is delta -
- hydrogen bonds are weak
Physical
- liquid
- ice is less dense
- solvent
- strong cohesion and surface tension properties
-high specific heat capacity
-high latent heat of vapourisation
-reactant
- transparent

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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.
Ice provides habitat

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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
Contains dissolved oxygen
Transport of substances

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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
Allows for transpiration stream

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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

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
what reactions creates a peptide bond between two amino acids
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)
26
what reactions breaks the peptide bond between two amino acids
hydrolysis addition of water and is used up
27
what is the primary structure of a protein
sequence of amino acid in a protein chain (polypeptide)
28
why is it important that the order of amino acids doesn't change in the primary structure
order determines the structure and shape of the protein and therefore the function
29
what is the secondary structure of an amino acid
chain of amino acid coils into an alpha helix or folds into a beta pleated sheet
30
what bond is in the secondary structure and what is it between
hydrogen bonds between the amino and carboxyl group of different amino acids 3D
31
what is the tertiary structure of a protein
overall 3D shape of a protein coils and pleats begin to fold in with areas of straight chains
32
what bonds hold the tertiary structure and in what shape
hydrogen, disulfide and ionic bonds between R groups very precise shape -globular proteins or fibrous proteins
33
what is the quaternary structure of a protein
more then one polypeptide chain and a non protein group
34
what bonds hold a quaternary structure
hydrogen, disulfide and ionic bonds
35
what do hydrogen bonds form between
form between hydrogen atoms with slight positive charge and other atoms with a slight negative charge
36
what groups in amino acids do hydrogen bonds form between
amino, carboxyl, hydroxyl groups
37
what is the role of hydrogen bonds
keeps tertiary and quaternary structure of protein in the correct shape provides strength
38
what do ionic bonds form between
carboxyl and amino groups part of the R group
39
what do ionic bonds do to the groups
ionises them into NH3+ and COO- strong attraction which forms bond
40
what do disulfide bonds form between and what type of bond is it
between the R groups of two cysteines containing sulfur strong covalent bond
41
what do hydrophobic parts of R groups do
associate in the center of the polypeptide to avoid water
42
what do hydrophilic parts of R groups do
associate near the edge of the polypeptide to be close to water
43
what do hydrophobic and hydrophilic interactions cause
twisting of amino acid chain results in protein changing shape
44
what are globular proteins
spherically shaped molecules which are soluble in water and have metabolic roles within an organism
45
how are globular proteins water soluble
has hydrophobic R groups turned inwards hydrophillic R groups on the outside so water molecules easily cluster around them and bind to them
46
what are fibrous proteins
a long, thin structure thats insoluble in water, metabolically inactive but provides structural roles within an organism
47
name 3 fibrous proteins
collagen keratin elastin
48
name 3 globular proteins
haemoglobin insulin pepsin
49
what is the function of collagen and name some specific examples
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
what is the function of keratin and why is it suited to its role
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
what is the function of elastin and why is it suited to its role
allows stretching/ adaption of shape in living things cross linking and coiling make it strong and extensible -skin, lungs, blood vessels
52
haemoglobin -structure -type of protein? -function/how it works
(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
what is the structure of insulin
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
how is insulin suited to its role
hydrophillic R groups = outside = soluble in water insulin binds to glycoprotein receptors
55
pepsin -function -structure -how is it suited to conditions
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
what is a prosthetic group
a non protein group that's permanently attached to a protein
57
what is a conjugated protein
a protein associated with a non protein group
58
what do carbohydrates contain
carbon hydrogen oxygen
59
what are the role of carbohydrates
source of energy store of energy structural units
60
what are monosaccharides
simplest carbohydrates
61
state the properties of monosaccharides
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
what are disaccharides and what are they joined by
two monosaccharides joined together by glycosidic bonds
63
name properties of disaccharides
sweet soluble
64
name 4 examples of disaccharides and what they are made of
alpha glu. + alpha glu. = maltose beta glu. + fructose = sucrose beta galactose + alpha glu.= lactose beta + beta = cellobiose
65
what reactions forms and breaks glycosidic bonds
condensation reaction hydrolysis
66
name a non reducing sugar
sucrose
67
name reducing sugars
maltose and lactose
68
what is the structural difference between alpha and beta glucose
the hydroxyl group and hydrogen on carbon 1 are reversed
69
what is the structural difference between ribose and deoxyribose
ribose has two hydoxyl groups on carbon 2/3 deoxy only has it on carbon 3
70
what type of sugar are alpha and beta glucose
hexose
71
what type of sugar is ribose and deoxyribose
pentose
72
what are polysaccharides
polymers of monosaccharides
73
what is homopolysaccharide and heteropolysaccharide
homo= same type of monosaccharides hetero= different types
74
describe the structure of starch and its function
alpha glucose in two different structural units -amylopectin -amylose storage of energy in plants insoluble
75
describe the structure of amylose
long chain of alpha glucose in coil shape 1-4 glycosidic bonds hydrogen bonds hold coil less soluble
76
describe the structure of amylopectin
long chain of alpha glucose 1-4 glycosidic bonds 1-6 glycosidic bonds = branched
77
describe the structure of glycogen and function
long chain of alpha glucose 1-4 glycosidic bonds 1-6 glycosidic bonds = branched compact act as energy store in animals insoluble
78
describe the structure of cellulose
homopolysaccharide of beta glucose 1-4 beta glycosidic bonds straight chain (hydroxyl and hydrgoen)reversed so straight chain insoluble
79
what is a phospholipid
2 fatty acids and a phosphate head joined to a glycerol backbone
80
how do phospholipids behave in water
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
what is a bilayer and what does it form
two layers of phospholipids membranes
82
what is cholesterol
steroid alcohol/ sterol which is a lipid not made of glycerol or fatty acids made of 4 carbon based rings
83
what is the role of cholesterol
provide stability/ regulate fluidity of membrane
84
what is a triglyceride
A glycerol and 3 fatty acids
85
What is the structure of a glycerol
3 carbon Each have one OH Filled with H
86
Which is more soluble amylose or amylopectin
Amylose
87
how to test for proteins
spotting tile pipette biuret solution blue to lilac
88
how to test for starch
spotting tile pipette iodine test brown/ range to blue/ black
89
how to test for lipids
test tube filter paper and funnel pipette Emulsion test + Reagents add ethanol mix with water filter and add water to filtrate clear/colourless to cloudy/ milky
90
how to test for reducing sugars
benedicts reagant heat coloured precipitate should form high concentration = brick red/brown
91
how to test for non reducing sugars
add hydrochloric acid and heat neutralise the solution with sodium hydrogencarbonate add benedicts and heat
92
how do you complete a serial dilution
distilled water stock solution use same volume to make each solution
93
explain how colorimetry works
zero/ calibrate with distilled water use a range of known (glucose) concentrations measure percentage transmission (light) absorption of glucose solution(s) by placing samples in cuvette red filter
94
how to find RF value
spot/solvent

module 2: foundations to biology (6 decks)

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