Year 1 Model Answers Flashcards
Describe Condensation Reactions
Monomers are joined together producing a larger molecule forming a bond.
A molecule of water is formed in this process
Describe Hydrolysis
Polymers and dimers are split a part breaking bonds
A water molecule is formed in this process
Name the bonds in biological molecules
glucose + glucose –>
glucose + galactose –>
glucose + fructose –>
glucose + glucose –> maltose (malt sugar)
glucose + galactose –> lactose (milk sugar)
glucose + fructose –> sucrose (table sugar)
Describe the structure and function of starch
Alpha glucose monomers
Polysaccharide
Has 1-4 glycosidic bonds
Amylose is helical
Amylopectin is branched and has additional 1-6 glycosidic bonds
Insoluble so doesn’t effect water potential
Branched so accessible for respiration
Describe the structure and function of glycogen
Alpha glucose monomers
Polysaccharide
Has 1-4 glycosidic bonds
Is branched and has many additional 1-6 glycosidic bonds
Highly branched so accessible for respiration
Describe the structure and function of cellulose
Beta-glucose monomers
Polysaccharide
Has 1-4 glycosidic bonds with alternating molecules being rotated by 180 degrees
Straight, unbranched chains
Straight chains ideal for cell wall, have crosslinks for stability
Describe the test for reducing sugars
Add Benedict’s reagent
Boil in a waterbath
Brick red colour indicates a reducing sugar
E.g. glucose
Describe the test for a non-reducing sugar
Carry out benedict’s test and see a negative result
Boil in a water bath with hydrochloric acid
Neutralise the acid with sodium hydrogen carbonate
Carry out Benedict’s test – a brick red result indicates a reducing sugar.
E.g. sucrose (this is the only one you need to remember)
Describe the test for starch
Add iodine to food sample
Blue/Black indicates starch is present
Describe the structure of amino acids and how they are joined
Amino acids contain C, O, H and N
They have a carboxyl group and an amine group
They also have an R group which can change the properties of the amino acid
There are 20 amino acids
They react in a condensation reaction and are joined by a peptide bond
A polymer of amino acids is called a polypeptide
Describe protein structure
Proteins have a primary structure that is formed by a sequence of many amino acids that are joined by peptide bonds in a condensation reaction
The primary structure folds into a secondary structure of either alpha helix or beta pleated sheets and these are held together by hydrogen bonds
The secondary structure further folds into a tertiary 3D structure that is held together by hydrogen bonds, ionic bonds and disulphide bonds
Some proteins e.g. antibodies may form a quaternary structure of more than one polypeptide chain(some of these may have prosthetic groups e.g. haem)
Describe the test for protein
Add Biurets reagent to sample (copper sulphate and sodium hydroxide)
Mix and heat
Lilac colour indicates protein is present
Describe the structure and function of triglycerides
Condensation of one glycerol and three fatty acids forming and ester bond
Fatty acids have an R group that can be saturated(C-C) or unsaturated (C=C)
Triglycerides are non-polar
Insoluble
Can’t form a bilayer
Used for longer term energy storage
Describe the structure and function of a phospholipid
Condensation reaction forming ester bonds
One glycerol and two fatty acids
One fatty acid is replaced by a phosphate group
The phosphate group is polar
The fatty acids are non-polar
Insoluble
Used in the phospholipid bilayer
Describe the emulsion test
Mix sample with ethanol and shake
Add water
If lipid is present a milky white emulsion will be seen
Describe enzyme induced fit
Enzyme active site is complementary to the substrate
When substrate binds the enzyme changes shape slightly
This stresses the bonds in the substrate
Reducing the activation energy for the reaction
The reaction occurs quicker
Describe competitive inhibitors
Binds to active site
Blocks active site so substrate can’t bind
Fewer enzyme-substrate complexes form
Describe non-competitive inhibitors
Binds to allosteric site
Changes tertiary structure
Enzyme is no longer complementary to substrate
Fewer enzyme-substrate complexes form
Describe DNA structure
DNA is made of a polymer of nucleotides/polynucleotide
It is two molecules that are antiparallel to each other coiled into a double helix.
Each nucleotide is made of deoxyribose, a phosphate group and a nitrogenous base that can either be adenine, cytosine, thymine or guanine
The adjacent nucleotides are joined to each other between the sugar and phosphate groups in a condensation reaction forming a phosphodiester bond
Complementary base pairing holds the two strands together due to hydrogen bonds forming between A - T and C - G.
Describe DNA replication
DNA helicase breaks the hydrogen bonds causing the strands to separate
Both strands act as a template
Free nucleotides complementary base pair to the template A-T and G-C
DNA polymerase joins adjacent nucleotides together forming a phosphodiester bond
Hydrogen bonds form between the old strand and the newly synthesised strand
DNA replication is semi-conservative replication
Describe ATP structure
DNA helicase breaks the hydrogen bonds causing the strands to separate
Both strands act as a template
Free nucleotides complementary base pair to the template A-T and G-C
DNA polymerase joins adjacent nucleotides together forming a phosphodiester bond
Hydrogen bonds form between the old strand and the newly synthesised strand
DNA replication is semi-conservative replication
Describe the properties of water
It is a metabolite in hydrolysis/condensation reactions
A solvent so metablic reactions can occur
High specific heat capacity to buffer changes in temperature
High latent heat of vaporisation providing a cooling effect
Cohesion between molecules forms a continuous column of water in the xylem and surface tension for organisms to move on bodies of water
Describe 3 of the inorganic ions you need to know in A level Biology
Inorganic ions are dissolved in bodily fluids and cytoplasm
They typically have a specific role
H+ For Chemiosmosis and Oxidative phosphorylation and maintaining pH
Fe2+ Haemoglobin
Na+ Co-transport, depolarisation, sodium potassium pump in action potentials
K+ For sodium potassium pump
Ca2+ For NMJ, synaptic transmission and sliding filament
PO43- For phospholipid bilayer, DNA, RNA and ATP
NO3- For N-cycle and Nitrogen containing compounds e.g. amino acids, DNA, ATP etc
Describe adaptations of cells
Depends a lot on the context, but…
Many mitochondria for increased rates of aerobic respiration and ATP production
Microvilli to increase the surface area of the cell surface membrane to increase the rate of diffusion
More carrier proteins to increase the rate of active transport
More ribosomes to produce more proteins
Describe how and optical microscope works and the advantages and disadvantages of them
Light passes through the specimen so it needs to be a thin layer of cells
Has lower magnification
Lower resolution as the wavelength of light is too long (some organelles may be missed)
Can view live specimens
Can show images in colour via staining
Not very complex preparation
Name the viral structures
A Attachment protein (binds to a receptor on host cell e.g. CD4 in HIV)
B Enzymes e.g. reverse transcriptase
D Genetic Material (RNA in HIV)
E Lipid Envelope
F Protein Capsid
Describe how an electron microscope works and the advantages and disadvantages of them
Electrons pass through the sample so it must be sliced thinly
Higher magnification
Higher resolution as the wavelength of electrons is shorter – so we can see smaller objects
Artifacts may be present
Can’t view live specimens
Can’t see colour images
Complex preparation
SCANNING shows 3D surface of the cell
TRANSMISSION shows a cross sections of the cell
What happens if the temperature is above an enzymes optimum
Too much kinetic energy
Breaks the hydrogen and ionic bonds
Tertiary structure denatures
Active site changes shape and the enzyme substrate complex can’t form
Reaction slows to a stop
What happens if the temperature is below an enzymes optimum
Not enough kinetic energy
Enzymes substrate complexes don’t form
Reaction slows
What happens to a reaction as you increase the substrate concentration
The reaction increases as the concentration of substrate increases
Eventually the rate plateaus as the reaction is limited by the number of enzymes
The active sites become saturated
What happens to a reaction as you increase the enzyme concentration
The reaction increases as the concentration of enzyme increases
Eventually the rate plateaus as the reaction is limited by the substrate concentration