what is the order of the conversion of units
nano - n
micro - μ
milli - m
no prefix
kilo - k
how do you go from a smaller to a bigger number
divide by 1000
how do you go from a bigger to a smaller number
multiply by 1000
what are pipettes
precision instruments that can accurately measure liquid volumes in the microliter range
what is the volume adjustment wheel
is used to set the volume that the pipette will despense
what is the volume display window
the volume that will be delivered is shown here in 3 numbers
what is the volume range
the range of volume a pipette can accurately measure is shown on top of its plunger button
what is the measurement error rate if the maximum volume of the pipettes we use in BIOC 192
~1%
why are solutions diluted
solutions are often too strong (concentrated) to be analyzed accurately, so they have to be diluted to a weaker concentration before analysis
what is the dilution factor
how much a solution is diluted
what will the dilution factor depend on
will depend on how concentrated the initial solution is
what is the equation for DF when you know the volume of your solution
DF = final total volume/volume of undiluted solution
what is the equation for DF when you know the concentration of your solution
DF = undiluted concentration/diluted concentration
what formula can you use when you don’t know the dilution factor
c1 * v1 = c2 * v2
what happens to denatured proteins
they lose their native structure and therefore cannot carry out their function
how can the making and breaking of bonds cause disruption if that is how proteins are regulated
ABNORMAL disruptions of even a small number of bonds can result in a denatured, no functional protein
what did Anfinsen’s experiment with ribonuclease show
that proteins can be unfolded (denatured) and refolded (to their native conformation) by changing the environment of the protein
how can factors and environmental conditions affect protein folding
factors can lead to protein unfolding decrease the strength of the bonds that stabilize folded proteins
what is the changes in structure associated with
gain (folded) and loss (unfolded) of protein function
what factors can affect protein structure and stability
heat, pH and ionic strength
how does heating the protein affect the protein
heating a protein will increase the kinetic energy of the proteins’ molecules. when enough heat energy is added to molecules they start to rapidly vibrate. this causes any weaker, non covalent interaction to be disrupted. the breaking of non covalent interactions in a protein can be destabilize the structure and cause the protein to denature
how can denaturing be cause by pH changes
the ionization states of ionizable amino acid side chain can change as a function of pH, resulting in denaturation of the protein structure in more acidic or basic conditions. at low pH, ionizable amino acid side chain become protonated, while at high pH they become deprotonated. pH induced alteration of the ionization status of a protein will result in the disruption of non covalent interaction hat would normally stabilize the protein fold
what is salivary (alpha) amylase
is an enzyme that breaks down carbohydrates in the mouth, digesting starch
what happens to the salivary amylase once it reaches the stomach
when food is consumed a strong acid (HCl) is release into the stomach, reducing the stomach pH from ~5.5 pre-food to below 3. this leads to the unfolding and inactivation of salivary amylase as it enters the stomach.