topic one - biological molecules - mr hedditch Flashcards

1
Q

4 important ways of water to living organisms?

A

chemical reactions
hydrolysis reaction
excretion
photosynthesis

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2
Q

draw a water molecule?

A

2-H positive 1-O negative

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3
Q

draw hydrogen bonding?

A

4-H positive 2-O negative lines between bonds

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4
Q

what happens in hydrogen bonding?

A

oxygen attracts hydrogen bond as it is negative and hydrogen is positive

there is a weak link between the bonds showing that it can be easily broken

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5
Q

what does the ‘delta’ sign mean?

A

indicates a slight change

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6
Q

why is having a high boiling point and high specific heat capacity good and bad (water)?

A

good - keeps the heat/temp stable and cools down slowly

bad - needs large amount of energy to increase the temp of water

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7
Q

why does ice float on water and how is this useful?

A

it floats on water because ice is more dense than water

it useful because things don’t sink e.g. polar bears living in the arctic

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8
Q

why is water a good solvent for molecules?

A

waters polarity allows it to dissolve both ionic bonds and other polar molecules

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9
Q

what is cohesion and what does it create?

A

water molecules sticking together

this creates surface tension at the water surface

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10
Q

what is cohesion useful for?

A

plant transport

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11
Q

give examples of 4 biological molecules?

A

carbohydrates
proteins
liquids
nucleic acid

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12
Q

define ‘monomers’

A

small, basic molecules that are the building blocks for larger molecules

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13
Q

define ‘polymer’

A

large complex molecules made of many monomers joined together

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14
Q

what type of reaction are polymers joined together by?

A

a condensation reaction

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15
Q

what bond is made when polymers form?

A

a covalent bond

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16
Q

how are polymers broken down into polymers?

A

through a hydrolysis reaction

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17
Q

state three roles carbohydrates has towards organisms?

A

acts as an energy source for respiration e.g. glucose
acts as an energy store e.g. starch
structure role e.g. cellulose in plant cell walls

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18
Q

what does saccharide mean?

A

a sugar

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19
Q

define ‘monosaccharide’ + example

A

a simple sugar made up of one bond e.g. glucose

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20
Q

define ‘disaccharide’ + example

A

a sugar composed of two monosaccharides e.g. lactose

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21
Q

define ‘polysaccharide’ + example

A

a complex carbohydrate e.g. starch

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22
Q

define ‘ribose’

A

a monosaccharide formed from five carbon atoms - pentose sugar

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23
Q

what is the difference between glucose alpha & beta?

A

in Alpha-glucose H is Above and the OH is below however in the Beta-glucose H is Below and the OH is above

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24
Q

state three of glucose’s functions?

A

readily respired to release energy
small molecule - enter cells easily by diffusion
soluble - easily transported around organism

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25
draw alpha-glucose
diagram
26
draw beta-glucose
diagram
27
what is a glyosidic bond?
the bond formed between to monosaccharides
28
what is starch a polymer of?
alpha-glucose
29
is starch insoluble in water? if so why?
no, because it consists of two polymers
30
starch is made up of two types of molecules, what are they?
amylose | amylopectin
31
define 'amylose' and state how much amylose is in starch?
it's a simple poly-(1,4) alpha-glucose, it's a straight chain molecule it makes up 80% of starch
32
what shape does the amylose chain curl up into?
a helix shape
33
define 'amylopectin' and state how much amylopectin is in starch?
it's a poly -(1,4) alpha-glucose and makes up 4% of starch
34
amylopectin gives a more open structure than amylose, suggest why?
it has more ends and can be hydrolysed more quickly than amylose by amylase enzymes
35
what is sucrose made up of?
alpha-glucose and fructose
36
what is maltose made up of?
two alpha-glucose's
37
what is lactose made up of?
galactose and alpha-glucose
38
draw maltose
diagram - check with diagram sheet in book | make sure H2O is on the side
39
draw sucrose
diagram - check with diagram sheet in book | make sure H2O is on the side
40
draw lactose
diagram - check with diagram sheet in book alpha should be flipped make sure H2O is on the side
41
lipids are a varied and diverse group of substances | that share characteristics, state these?
containing carbon, hydrogen & oxygen the proportion of oxygen to carbon and hydrogen is smaller than in carbohydrates they are insoluble in water (non-polar molecule) they are soluble in organic solvents such as alcohols and acetone
42
what are the main group of lipids, and what is it?
triglycerides, it fats and oils
43
state the uses of lipids?
energy source (for respiration)/energy store thermal insulation e.g. blubber in polar animals electrical insulation e.g. around the axon of neurones biological membranes hormones waterproofing protection e.g. reducing transpiration from leaves; vital organs in animal
44
difference between fats and oils?
fats are solid at room temp oils are liquid fats are saturated oil are unsaturated
45
what's does a triglyceride molecule consist of & how is it formed?
a triglyceride molecule consists of a glycerol molecule, and three fatty acid chains the fatty acids are joined to the glycerol molecule by ester bonds formed by condensation reactions.
46
what's a glycerol made of?
glycerol is a 3-carbon molecule with 3 –OH groups
47
define 'fatty acids' and explain the bonds?
fatty acids are a long chain of hydrocarbons with a carboxyl group at one end unsaturated - double bonds saturated - single bond
48
why are triglyceride insoluble in water?
triglycerides are insoluble in water (hydrophobic) | because they are non-polar molecules
49
state the main role of a triglyceride?
to store energy for later use
50
draw diagrams to show the structure of a glycerol molecule, and a fatty acid chain that is 8 C-atoms long
check biology book
51
where is amylose, amylopectin, glycogen & cellulose found in?
amylose - plants amylopectin - plants glycogen - animals cellulose - plants
52
what is amylose, amylopectin, glycogen & cellulose found as?
amylose - grains amylopectin - grains glycogen - granules cellulose - fibre
53
what is the functions of amylose, amylopectin, glycogen & cellulose?
amylose - energy store amylopectin - energy store glycogen - energy store cellulose - structural support
54
what are the basic monomer units for amylose, amylopectin, glycogen & cellulose?
amylose - alpha-glucose amylopectin - beta-glucose glycogen - alpha-glucose cellulose - beta-glucose
55
what are the types of bonds between monomers for amylose, amylopectin, glycogen & cellulose?
amylose - glycosidic bond (1,4) amylopectin - glycosidic bond (1,4 + 1,6) glycogen - glycosidic bond (1,4 + 1,6) cellulose - glycosidic bond (1,4)
56
what are the types of chains for amylose, amylopectin, glycogen & cellulose?
amylose - unbranched & curls to helix amylopectin - long, few branches glycogen - short, lots of branches cellulose - chains of long unbranched monomers
57
describe the structure of phospholipids?
consists of a glycerol molecule, a phosphate group & two fatty acids
58
apart from a phosphate group and two fatty acids, which other component makes up a phosphide molecule?
glycerol
59
elements found in lipids?
carbon, hydrogen, oxygen
60
name the class of hormones made of cholesterol molecules?
steroid hormones
61
what is the role of cholesterol in plasma membrane?
regulates how fluid it is & forms the basis of steroid hormones
62
which property of phosphide molecules makes them well suited to their role in plasma membrane?
some are hydrophobic & some are hydrophilic
63
which elements do proteins contain?
carbon, hydrogen, oxygen and sometimes nitrogen
64
name the importance's of proteins?
structure - collagen, muscle mass enzymes - catalyse a range of reactions transport - membrane carriers
65
define 'amino acids' name some of the common structures?
are monomers that form dipeptides & protein common structures are: a central carbon atom a side chain or R-group
66
draw an amino acid?
check with book
67
what is the R-group, which is the simplest amino acid and what kind of atom is the R-group?
the R-group gives each amino acid unique properties which make it different from the other amino acids, the simplest amino acid is glycine and the R-group is made from a hydrogen atom
68
how many amino acids are there?
20
69
how are dipeptides formed and what happens in this process?
through a condensation reaction between two amino acids the water molecule is eliminated and a peptide bond is formed
70
how can a dipeptide bond broken?
by adding water (hydrolysis)
71
define 'polypeptides' and where does it take place?
long chains of amino acids joined together by peptide bonds takes place in the ribosomes
72
define what is meant by a 'primary structure of proteins'?
is the specific sequence of amino acids in a polypeptide chain
73
define what is meant by a 'secondary structure of proteins'?
the coiling or folding of the polypeptide chain due to the formation of the hydrogen bonds
74
what are the two main three-dimensional shapes formed from the secondary structure?
alpha helix | beta pleated sheets
75
define 'alpha helix'?
the H on the –NH group are attracted to the O on the –CO group the H is slightly positive and the O is slightly negative a hydrogen bond forms between these two atoms the polypeptide chain coils up into a helical shape
76
define what is meant by 'tertiary structure of a protein'?
overall 3D shape of a protein molecule
77
name the four types of bonding involved in tertiary structure?
hydrogen bonds ionic bonds disulphide bonds hydrophobic and hydrophilic interactions
78
state the two main 3D proteins formed in the tertiary structure?
fibrous e.g. collagen | globular e.g. haemoglobin
79
define the 'quaternary structure?
the way that two or more polypeptide subunits are arranged to give a final specific shape e.g. insulin, collagen & haemoglobin
80
what shape are globular protein and why?
globular proteins are round in shape and compact because of the tendency of hydrophobic R-groups to cluster on the inside of the molecule while the hydrophilic R-groups stay on the outside
81
examples of globular proteins?
haemoglobin pepsin insulin
82
what is haemoglobin?
haemoglobin is a globular transport protein. It binds | with oxygen in the lungs to form oxyhaemoglobin
83
what do haemoglobin consists of?
consists of four polypeptide sub-units two are an identical pair called alpha-chains, and two are a different identical pair called beta-chains disulphide bonds hold the chains together
84
what does each subunit contain?
each subunit contains a haem group - an inorganic iron ion (Fe2+)
85
what are proteins with prosthetic group called and what is a prosthetic group?
proteins which have a prosthetic group are called conjugated protein permanent parts of a protein molecule but are not made of amino acids are called prosthetic groups
86
define pepsin?
a digestive enzyme found in the stomach
87
define insulin?
a hormone secreted by the pancreas. It is essential in the regulation of blood glucose levels
88
define a fibrous protein?
are tough and rope-shaped, they are insoluble, unreactive and mechanically strong – essential properties for structural role
89
state the three examples of fibrous protein?
collagen keratin elastin
90
define the structure collagen and where its found?
consists of three polypeptide chains, each in the shape of a helix (NOT an alpha-helix though) these three chains are wound around each other to form a rope-like structure, held in place by hydrogen bonds ``` in connective tissues: skin bone teeth walls of blood vessels etc. ```
91
define keratin and give examples of where its found?
as keratin is insoluble it provides a waterproof barrier and helps stop pathogens entering the body ``` found in nails hair/fur claws horns hooves scales feathers ```
92
define what elastin is and does?
it is elastic – it stretches as tissues expand and then recoils to allows the tissue to return to its original shape
93
what is denaturation in proteins?
It loses its shape permanently (tertiary structure is | damaged). This means the protein will no longer function properly
94
what causes denatured proteins?
heat – increased kinetic energy breaks hydrogen bonds and disrupts hydrophobic interactions acids/bases – H+ or OH-ions break hydrogen bonds between polar R-groups and break ionic bonds heavy metal ions – react with disulphide bonds to form solid
95
what are inorganic ions?
ions are atoms or molecules with an electrical charge Inorganic ions do not contain carbon atom
96
what are positive and negative ions called?
positive - cathode | negative - anode
97
what are the key inorganic positive ions in biological molecules?
``` calcium ions (Ca2+), sodium ions (Na+), potassium ions (K+), hydrogen ions (H+), ammonium ions (NH4+) ```
98
what are the key inorganic negative ions in biological molecules?
nitrate (NO3–), hydrogen carbonate (HCO3–), chloride (Cl-), phosphate (PO43–), hydroxide, (OH)
99
steps of chromatography?
there are two components of chromatography: stationary phase - the chromatography paper (made If cellulose) or TLC plate mobile phase - a liquid solvent water for polar molecules ethanol for non-polar molecules the mobile phase moves up the stationary phase the different molecules in the the mixture moves at different speeds up the paper depending on there solubility, polarity and size the paper/plate is removed from the solvent when the solvent front is roughly at the top the pattern of spots made by the different molecules is called a chromatogram
100
what is chromatography is used for?
used to separate out molecules in a mixture
101
what the two main types of chromatography?
paper chromatography | thin - layer chromatography (TLC)
102
application of TLC?
monitor the process of chemical reactions urinalysis- testing for banned drugs in spots testing the purity of drugs testing foods for contamination
103
state the six qualitative tests?
monitor the process of chemical reactions urinalysis- testing for banned drugs in spots testing the purity of drugs testing foods for contamination
104
postive results for starch?
brick red
105
postive result for protein?
forms a cloudy red precipitate
106
postive result for lipids?
black
107
postive results for reducing sugars?
lilac
108
state the 10 stages of determining glucose?
Label five boiling tubes 0.1%, 0.5%, 1.0%, 1.5% and 2.0% glucose (mass (g) per volume (dm3)). 2. Using a clean syringe, add 5cm3 Benedict’s reagent to each tube (Benedict’s must be in excess so that all of the sugar reacts) 3. Add 0.5cm3 of each of the glucose solutions to the labelled boiling tubes, using a clean syringe each time. 4. Stir each with a clean dry glass rod. 5. Heat all the boiling tubes into a water bath at 80°C for ten minutes. 6. Carefully remove the tubes from the water and allow to cool. 7. Remove the precipitate, using filtration or a centrifuge 8. Pipette the remaining liquid (supernatant) into clean cuvettes before placing in the colorimeter (no fingerprints!) 9. Put a red filter into the colorimeter (as sample is blue) 10. Take one colorimeter reading for each cuvette. Remember to calibrate the colorimeter (set it to 100% transmission) between each reading using a cuvette of water – a “blank”
109
what can quantitative tests tell us?
whether a solution contains a certain type of molecule, but not how much is present
110
what can the benedicts test us?
the Benedict’s test can give us an idea of whether a solution contains no reducing sugars, a small amount or a large quantity, based on the degree of colour change
111
What are the limitations of qualitative testing?
only gives you a yes or no result, it doesn’t give you a numerical value
112
Why did you use water as a control in each of your tests?
because distilled water doesn’t contain anything – won’t affect the outcome of tests
113
What would you need to do if you wanted to test a solid | substance?
grind substance and add distilled water to add fluidity
114
What is meant by a “reducing sugar”?
include all monosaccharides and disaccharides and they are known as reducing sugars because they can give electrons to other molecules
115
Why must you check there is no reducing sugar in a sample before testing for the presence of a non-reducing sugar?
because non reducing sugars don’t change the colour of the solution – this has led to sugar breakdown to monosaccharides by hydrolysis
116
# Define the following terms: a) Reduction b) Emulsion c) Precipitate
the gaining of electrons two or more liquids in which one is present as droplets causing a solid to settle out of a solution
117
Why would a solution of amino acids give a negative result for the Biuret test?
when there no peptide bonds
118
Why do lipids form an emulsion in water?
lipids are insoluble in water and soluble in ethanol then added to H20 something tiny dispersed droplets in water