biology paper 1 Flashcards
what is a monomer
a repeating simple molecular unit
hydrolysis reaction and condensation rection definitions important and on
hydrolysis - breaks a chemical bond
condensation reaction - forms a chemical bond
which part of 2 alpha glucoses for a glycosidic bond
the OH on one and the H on the others OH
biochemical test for a non reducing sugar
- heat with HCL
- neutralize with NaOH
- heat with benedicts solution
- pos result is a brik red ppt from a clue solution
(can be a different color depending on conc)
why the use of a colorimeter improves the repeatability of the results for a benedicts
quantitative result
standardizes the method
instead of using a colorimeter how workout the quantity of reducing sugar in the solution
- filter and dry the ppt
- find the mass/ weight (weigh it)
disaccharides (3 of them)
sucrose - glucose and fructose
lactose - galactose and glucose
maltose - glucose and glucose
differences between cellulose and glycogen
cellulose beta glucose AND glycogen is made of alpha glucose
cellulose is straight chain AND glycogen is branched
cellulose is straight chain AND glycogen is coiled
2 features of starch that make it a good storage molecule
- insoluble in water - so doesn’t effect water potential
- coiled - make the molecule compact
- branched - more endos for faster break down action as more enzymes can attach
glycogen acting as a source of energy
hydrolyzed into alpha glucose
glucose is used in respiration to make ATP
difference in starch and cellulose from the finger
displacement reactions with group 7 17
ionic titrations
starch adapted to function in a plant cell
insoluble - doesn’t effect water potential
helical - compact
large molecule - cant leave the cell
emulsion test
- add ethanol
- shake
- THEN add water
pos : milky white emulsion
important thing to remmeber if it asks you how to calculate a percentage
must state multiply by 100 at the end
what peptidase hydrolysis the peptide bond that is not at the end
endopeptidase
anything enzyme questions
COMPLIMENTRY
Induced fit modle and enzyme action as a catalyst
- Substrate binds to active site
- Enzyme substrate complex is formed
- Active site changes shape slightly so that is complimentary to the substrate
- Reduces the activation energy
Procedure to stop an enzyme catalysed reaction
Boil or add a strong acid/alkali to denatured the enzyme
Or freeze.
So no collisions as lower ke meaning no complexes formed
Enzyme questions important point
Enzyme - substrate complexes
Weight gain questions
Less hydrolysis of starch
Less maltose
Meaning Less absorption of glucose
Means Less weight gain
how an active site if an ezyme causes a high rate of reaction
- lowers activation energy
- induced fit causes active site of the enzyme to change
- enzyme substrate complex of formed - cause bond to form / break/ causes strain on the bonds
protein test
- add biuret reagent
- pos result = purple
similarity and differences between dipeptides
similarity
consists of two amino acids
joined by a peptide bonds
all made of amino acids with a amine group
all made of amino acids with a carboxyl group
two r groups
contain carbon ad hydrogen and nitrogen and oxygen
difference
differ in the amino acid they contain
amino acids diffrent r groups
why non competitive inhibitor
because as substrate concentration increases rate stays the same - as the enzymes have been denatured
how peptide bond formed
condensation reaction between the amine group of one ammino acid and the carboxylic group of another
enzyme substrate complexes
reduces the activation energy
due to bending bonds
non completive inhibitor - can increase rate
bond alters the tertiary structure of the enzyme
causes the active site to change
more successful enzyme substrate complexes
when DNA helicase breaks the hydrogen bonds
DO NOT write HYDROLYSIS
role of single stranded template in DNA replication
determine the order of nucleotides in the complimentary new strand