BIO 212 LAB EXAM 1 QUESTIONS AND ANSWERS
Which substances allows proteins to be sorted by size after they are denatured? -
Answers - polyacrylamide
SDS works on protein by? - Answers - adding negative charges
which level of protein structure remains after denaturation for SDS PAGE? - Answers -
primary
If you have a dimer protein which has 2 subunits each 30kDa. How many bands or lines
would you see after SDS PAGE? - Answers - 1
What type of graph can be used to determine protein size? - Answers - linear semi log
graph
which chemical stains proteins so we can read their absorbance in the
spectrophotomerter? - Answers - Coomassie blue
a graph has A on the Y-axis and wavelength, its shape would be? - Answers - no
particular shape, we are trying to find the wavelength that yields the highest absorbance
If a sample was diluted 1/5 and the diluted sample was found to be 5mg/mL, what is the
undiluted concentration? - Answers - 25mg/mL
true or false, we expected all 1/50 dilutions of any cellular fraction/organelle to have the
same absorbance and protein concentration? - Answers - False
Which graph uses lambda max? - Answers - standard curve
As the substrate level increases, initially the velocity will increase until the enzyme
active sites are full for a population of that enzyme. This is when the enzyme reaches? -
Answers - Vmax
The part of the enzyme that binds the substrate or reactant and performs catalysis is
called? - Answers - active site
In our experiment, sodium azide allowed us to measure blank of DCPIP to estimate
velocity of succinate dehydrogenase? - Answers - reduction
which of the following conditions would not lead to low or no activity of the enzyme
Succinate dehydrogenase? - Answers - incubation at 30 degrees Celsius
a competitive inhibitor? - Answers - increases Km
Which substances allows proteins to be sorted by size after they are denatured? -
Answers - polyacrylamide
SDS works on protein by? - Answers - adding negative charges
which level of protein structure remains after denaturation for SDS PAGE? - Answers -
primary
If you have a dimer protein which has 2 subunits each 30kDa. How many bands or lines
would you see after SDS PAGE? - Answers - 1
What type of graph can be used to determine protein size? - Answers - linear semi log
graph
which chemical stains proteins so we can read their absorbance in the
spectrophotomerter? - Answers - Coomassie blue
a graph has A on the Y-axis and wavelength, its shape would be? - Answers - no
particular shape, we are trying to find the wavelength that yields the highest absorbance
If a sample was diluted 1/5 and the diluted sample was found to be 5mg/mL, what is the
undiluted concentration? - Answers - 25mg/mL
true or false, we expected all 1/50 dilutions of any cellular fraction/organelle to have the
same absorbance and protein concentration? - Answers - False
Which graph uses lambda max? - Answers - standard curve
As the substrate level increases, initially the velocity will increase until the enzyme
active sites are full for a population of that enzyme. This is when the enzyme reaches? -
Answers - Vmax
The part of the enzyme that binds the substrate or reactant and performs catalysis is
called? - Answers - active site
In our experiment, sodium azide allowed us to measure blank of DCPIP to estimate
velocity of succinate dehydrogenase? - Answers - reduction
which of the following conditions would not lead to low or no activity of the enzyme
Succinate dehydrogenase? - Answers - incubation at 30 degrees Celsius
a competitive inhibitor? - Answers - increases Km
