|
Hint
|
Answer
|
|
What are phospholipids used as
|
structural components
|
|
What are most lipids made up of
|
fatty acids combined with an alcohol
|
|
Describe the structure of a fatty acid
|
carboxyl group attached to a hydrocarbon chain
|
|
what has a hydrocarbon chain saturated with hydrogen, with no carbon-carbon double bonds
|
saturated fatty acids
|
|
what has a hydrocarbon chain with at least one carbon-carbon double bond, causing the chain to kink
|
unsaturated fatty acids
|
|
How can you test for lipids
|
ethanol shake distilled water
|
|
What is the primary function of triglycerides
|
to store energy
|
|
What is the structure of a triglyceride
|
glycerol attached to 3 fatty acid tails
|
|
What are the components of a phospholipid
|
glycerol, phosphate, 2 fatty acid tails
|
|
What are the similarities between triglycerides and phospholipids
|
contain glycerol, fatty acids and ester bond
|
|
insoluble in water
|
|
contain carbon hydrogen and oxygen
|
|
What are the roles of proteins
|
enzymes and antibodies/transport and structural components/hormones and muscle contraction
|
|
What determines the properties of an amino acid
|
the R group
|
|
What type of bond joins amino acids together
|
peptide bonds
|
|
what do you call two amino acids joined by a peptide bond
|
dipeptide
|
|
Which test can identify proteins
|
biuret
|
|
What does the Biuret test detect
|
presence of peptide bonds
|
|
What does a blue colour indicate in the Biuret test
|
no proteins are present
|
|
what colour indicates present proteins
|
purple
|
|
What type of bonds are involved in the secondary structure of a protein
|
hydrogen bonds
|
|
What are the two possible shapes formed by a protein's secondary structure
|
alpha helix
|
|
beta pleated sheet
|
|
What holds the tertiary structure of a protein together
|
hydrogen and ionic bonds
|
|
disulphide bridges
|
|
hydrophobic and hydrophilic interactions
|
|
What are the weak interactions between polar and non-polar R groups called
|
hydrophobic and hydrophilic interactions
|
|
which structure has two or more polypeptide chains held together by bonds
|
quarternary
|
|
What are non-protein groups added to the quaternary structure called
|
prosthetic
|
|
which structure is the unique sequence of amino acids in the polypeptide chain
|
primary
|
|
which structure is the folding of the polypeptide chain into an alpha-helix or a beta-pleated sheet
|
secondary
|
|
which structure is the complex 3D structure formed by the folding and twisting of the polypeptide chain
|
tertiary
|
|
Which type of chemical bond forms between positive and negative R groups
|
ionic
|
|
How do enzymes speed up reactions
|
lower the activation energy
|
|
what is it when a substrate(s) binds to an enzyme
|
enzyme substrate complex
|
|
What is formed during an enzyme-catalysed reaction
|
products
|
|
which enzymes act within the cells that produce them
|
intracellular enzymes
|
|
which model suggests that enzymes have a specific active site that perfectly fits the substrate(s)
|
lock and key
|
|
which model proposes that the enzyme's active site changes shape when the substrate(s) bind, putting a strain on the substrate's bonds and lowering the activation energy
|
induced fit
|
|
Name a factor that can cause an enzyme to denature
|
high temperature/extreme ph
|
|
Name factors that affect the rate of enzyme-controlled reactions
|
temperature and ph/substrate and enzyme concentration
|
|
in which solutions do H+ ions break ionic or hydrogen bonds and denature the enzymes
|
acidic
|
|
in which solutions do OH- ions break ionic or hydrogen bonds and denature the enzymes
|
alkaline
|
|
what increases the rate of reaction until eventually the rate of reaction plateaus
|
increasing substrate or enzyme concentration
|
|
what are molecules that bind to enzymes to reduce their activity
|
inhibitors
|
|
what do reversible inhibitors do
|
form weak bonds with the enzyme
|
|
what do irreversible inhibitors do
|
form strong bonds with the enzyme
|
|
what are molecules that bind to the active site of the enzyme
|
competitive inhibitors
|
|
what are molecules that bind to enzymes away from the active site
|
non competitive inhibitors
|
|
which inhibitors decrease the rate of reaction by preventing the formation of enzyme-substrate complexes
|
competitive
|
