LAB 1 Flashcards

(40 cards)

1
Q

what is the order of the conversion of units

A

nano - n
micro - μ
milli - m
no prefix
kilo - k

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2
Q

how do you go from a smaller to a bigger number

A

divide by 1000

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3
Q

how do you go from a bigger to a smaller number

A

multiply by 1000

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4
Q

what are pipettes

A

precision instruments that can accurately measure liquid volumes in the microliter range

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5
Q

what is the volume adjustment wheel

A

is used to set the volume that the pipette will despense

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6
Q

what is the volume display window

A

the volume that will be delivered is shown here in 3 numbers

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7
Q

what is the volume range

A

the range of volume a pipette can accurately measure is shown on top of its plunger button

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8
Q

what is the measurement error rate if the maximum volume of the pipettes we use in BIOC 192

A

~1%

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9
Q

why are solutions diluted

A

solutions are often too strong (concentrated) to be analyzed accurately, so they have to be diluted to a weaker concentration before analysis

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10
Q

what is the dilution factor

A

how much a solution is diluted

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11
Q

what will the dilution factor depend on

A

will depend on how concentrated the initial solution is

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12
Q

what is the equation for DF when you know the volume of your solution

A

DF = final total volume/volume of undiluted solution

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13
Q

what is the equation for DF when you know the concentration of your solution

A

DF = undiluted concentration/diluted concentration

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14
Q

what formula can you use when you don’t know the dilution factor

A

c1 * v1 = c2 * v2

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15
Q

what happens to denatured proteins

A

they lose their native structure and therefore cannot carry out their function

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16
Q

how can the making and breaking of bonds cause disruption if that is how proteins are regulated

A

ABNORMAL disruptions of even a small number of bonds can result in a denatured, no functional protein

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17
Q

what did Anfinsen’s experiment with ribonuclease show

A

that proteins can be unfolded (denatured) and refolded (to their native conformation) by changing the environment of the protein

18
Q

how can factors and environmental conditions affect protein folding

A

factors can lead to protein unfolding decrease the strength of the bonds that stabilize folded proteins

19
Q

what is the changes in structure associated with

A

gain (folded) and loss (unfolded) of protein function

20
Q

what factors can affect protein structure and stability

A

heat, pH and ionic strength

21
Q

how does heating the protein affect the protein

A

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

22
Q

how can denaturing be cause by pH changes

A

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

23
Q

what is salivary (alpha) amylase

A

is an enzyme that breaks down carbohydrates in the mouth, digesting starch

24
Q

what happens to the salivary amylase once it reaches the stomach

A

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.

25
which enzyme continues the digestion of starch when it reaches the small intestine
pancreatic amylase
26
what is the primary structure of salivary amylase
a monomeric protein whose single polypeptide chain comprises of 496 amino acid residues
27
what is the secondary structure of salivary amylase
includes a total of 20 alpha helices and 42 beta strands
28
how many domains does salivary amylase have
3 domains a, b and c
29
what is the structure of the A domain in salivary amylase
has a beta/alpha barrel structure made up of 8 antiparallel beta strands surrounded by 8 alpha helices it contains the active site, which includes 2 important ions Cl and Ca
30
what is the structure of the B domain in salivary amylase
forms a open loop with several helices
31
what is the structure of the C domain in salivary amylase
has a Greek key type structure
32
what stabilizes the 2ndary structure of salivary amylase
non covalent interactions
33
what stabilizes the tertiary structure of salivary amylase
is stabilized by 5 disulfide bonds
34
what is starch
a carbohydrate found in plants
35
what is the structure of starch
it consists of 2 different types of polysaccharides that form 2 different structural arrangements - one is linear but coiled = amylose - the other is the branched = amylopectin
36
which structure in starch can be exploited to test
amylose component in starch can be exploited to test for the presence of starch in a solution
37
what happens during a iodine starch test
a solution of iodine/potassium iodine is added to a solution suspected of to contain starch
38
what will happen if starch is present when iodine starch test is added to solution
when this solution is added to any amylose-containing solution the iodine will slip into the amylose coil, resulting in the formation of a dark blue-black color
39
what will happen if no starch is present when iodine starch test is added to solution
the amylose-iodine complex will not be able to form and the iodine will stay its original brown-orange state
40
when is starch not present in solution
when starch has been digested into smaller carbohydrate units