Section bank Physics And Chem Flashcards

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1
Q

How do you calculate the magnitude of an electric field? The passage says 4.5kV at a distance of 0.5m.

A

The intensity of a uniform electric field E is related to the voltage V divided by the distance d from which it applied. 4.5kV/0.5m = 9kV/m

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2
Q

Benzene -1,4-diol can be made into 2,5- dihydroxybenzoic acid by what process?

A

By carboxylation. Notice that the numbering changes because of the importance of the carboxylic acid. And that the numbering starts from the alpha carbon.

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3
Q

The MALDI-MS technique allows the separation through which feature?

A

The velocity is inversely related to the ion mass-to-charge ratio. The fastest ion are those with the smallest m/z ratio, these arrive first at the MS detector.

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4
Q

The value of the electromagnetic energy delivered during one pulse can be calculated by?

A

Multiplying the W by the seconds to give you the answer in Joules. This is because Watts equals Joules/Seconds.

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5
Q

During a form of finger printing proteolytic cleavage happens, what type of reaction is that?

A

It is a hydrolysis reaction.

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6
Q

The photoacoustic Calorimetry (PAC) and the classic calorimetry based on thermometers in that?

A

It enables the measurement of fast and localized heat transfer process.

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7
Q

What is the reading of the energy when an appropriate laser is used in an photoacoustic calorimeter?

A

Based on the energy conservation, if the appropriate laser is use, the reading of the energy meter would be equal to zero for a laser use to disassociate a particular chemical bond.

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8
Q

The photon energy is directly proportional to?

A

The photon energy is directly proportional to radiation frequency. The higher the frequency they higher the photon energy.

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9
Q

Based on the ray diagram shown, the focal length would be? The laser is 12cm away passing through a convex or converging lens and hitting a sample 4cm on the other side.

A

1/f= 1/12+1/4= 1/12+3/12= 4/12= 12/4=f F=3

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10
Q

Which extraction procedure will completely separate an amide from the by-product of the reaction between an anime and excess carboxylic acid anhydride?

A

Add 0.1 M NaOH to quench unreacted anhydride. Then add diethyl ether and separate the layers. The amide can be obtained from the ether layer by evaporating the solvent. The by-product of such reaction will be an acidic carboxylic acid and the excess unreacted material will also be acidic. Extraction with aqueous base will hydrolyze and extract both of these into the aqueous layer, leaving the neutral amide in the ether layer.

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11
Q

What are the SI prefix, standard forms, and symbols? For the scientific notation needed for the MCAT?

A

-12,-9,-6, -3, -2,-1 1, 2, 3,6,9, 12 ^ p, n, μ, m, c, d da, h, k, M, G, T

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12
Q

The time dependence of the potassium current through a cell membrane channel is subject to a constant of 80-mV. The Amps is 400•10^-12

A

Ohms law is I= V/R so R = 80•10^-3/ 400•10^-12 = 8•10^-2/4•10^-10 = 200MΩ

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13
Q

Make sure you know how phophatidyl cholines members of the phosphatides look like. And phosphatides as well.

A

Look them up

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14
Q

Liposomes can be difficult to?

A

Detect since they do not absorbe visible light and many molecules absorbe UV light. A experimental design that allows fluorescent due to be trapped inside during liposome formation is needed. They can then be detected using fluorescent spectroscopy.

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15
Q

How do you measure catalytic efficiency?

A

By examining the ratio of Kcat/Km the higher the value the more efficient the enzyme.

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16
Q

What does the behavior of liposomes labeled compound 1 and compound 2 if the results are stable when mixed and forms new liposomes when mixed tells you about them?

A

It means that compound 1 is under kinectic control whereas compound 2 is under thermodynamic control due to the fact that the latter achives its thermodynamically stable step more rapidly. The thermodynamic product is reversible thus it would mix to create the most homogenous and stable intermediate, whereas kinetic is irreversible!

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17
Q

What mass of the compound (MW= 800g/mol) is contained in the solution prepared liposomes that elute at 20mL by size-exclusion chromatography? The figure showing the elution profile shows that at 20mL the concentration was 10mL The passage also says that the compounds were synthesized from 1mL

A

0.10mM*1mL = 0.1 microL 0.1 microL *800g/mol = 80 microL

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18
Q

What is the electronic configuration of the Co(II) center found vitamin B12?

A

Co2+ is a dication formed by the loss of two electrons so the 4s2 are lost and the answer is [Ar]3d^7

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19
Q

which cation is most likely to be found place of Fe2+ in the square planar binding of hemoglobin?

A

Co2+ is closely related to Fe2+

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20
Q

The ATP-dependent phosphorylation of a protein target is catalyzed by which class of enzyme?

A

Kinases catalyze the transfer of phosphate groups from ATP to target proteins and are classified as transferases.

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21
Q

Which compounds are easily detected during experiments by bright colors?

A

The compounds with larger sets of conjugates double bonds.

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22
Q

nonpolar amino acids?

A

The nine amino acids that have hydrophobic side chains are glycine (Gly), alanine (Ala), valine (Val), leucine (Leu), isoleucine (Ile), proline (Pro), phenylalanine (Phe), methionine (Met), and tryptophan (Trp). Shown at the right is the structure of valine.

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23
Q

To elimate or reduce the interaction of the sidechains to accomplish this while having minimal impact is on the overall structure?

A

Change the charged amino acids to alanine.

24
Q

The bond that links monosacharides together in an oligosaccharide is what known as what type of bond?

A

The bond that links monosacharides together in an oligosaccharide is a special type of acetal linkage known as a glycoside bond.

25
Q

The induced-fit model refers to?

A

The induced-fit model of enzyme catalysis states that the active site of the enzyme changes shape upon substrate binding and only the proper substrate causes a change that initiates catalysis.

26
Q

When performing experiments to measure Kcat of an enzyme, the substrate concentration should be? Why?

A

Saturating. Because the Kcat is used to describe the rate-limiting step of catalysis under saturating conditions of substrate

27
Q

When experiments are performed on enzymes that display traditional Michaelis-Menten kinetics, what shape does the graph of Vo versus substrate concentration [S] have?

A

traditional Michaelis-Menten kinetics describes a hyperbolic dependence of Vo on substrate concentration.

28
Q

What happens to Km and Vmax during competitive, uncompetitive, and noncompetitive inhibition.

A

During competitive inhibition Km goes up and Vmax remains the same. During uncompetitive inhibition Both Vmax and Km decrease. During non competitive inhibition. Vmax decreases and Km remains the same.

29
Q

at pH 7 histadine would be?

A

At pH 7 histadine would be neutral. because histadine pka is 6.

30
Q

Complementary colors? In nm.

A

ROYGBIV Red (640-700 nm) complementary to green (450-560nm) Violet (400-450nm) complementary to Yellow (560-600nm) Blue (450-480nm) complementary to orange (600-640nm)

31
Q

how do you calculate the Km an inhibitor using the lineweaver-burkplot?

A

The x intercept over 1 would give you Km.

32
Q

What method is used to calculate the Vmax lineweaver-burkplot?

A

Vmax is determined as the inverse of the y-intercept of the graph showned.

33
Q

An active homotetramer of 35kDa has how many bases?

A

140kDa as a homotetramer

34
Q

Histine tagging (represented in the passage by His-tagged) and nickel column (Nickel-…) chromatography are what form of chromatography?

A

Affinity chromatography

35
Q

Each mole of NaDH can reduce how many moles of disulfide bonds?

A

One mole of NaDH can reduce one mole of disulfide bonds.

36
Q

A protein that binds to an anion-exchange column is positive or negative?

A

It is NEGATIVE

37
Q

The more negative the protein the more what is needed for elution?

A

The more negative the protein the more NaCl is needed for the elution.

38
Q

Which nucleotides are purines? Pyramidines? What is Uracil?

A

-All Gods are Pure- Adenine and Guanine are Purines so C and T are pyramidines. U is also a pyramidine

39
Q

Changes that convert a pair bases from AU to GC would?

A

Increase the satability of the molecule. The stability of both DNA and RNa depends on the number of GC bases contained with the folded structure.

40
Q

How do you Obtaine the melting temperature from a graph that specifies the thermal denaturation and that has fraction denatured on the y-axis and temperature on the x-axis?

A

The melting temeprateture in such a graph would be the temperature at which half of the molecules are denatured or the fraction folded is 0.5. Question 71 from physics and chem

41
Q

Repeat question 73, 75,86

A

Hola

42
Q

How do you calculate the catalytic effeciency?

A

Divide Kcat by Km the hiher the number the better. Remember that Km needs to be the smallest and Kcat the largest. Quickly try to make the approximations.

43
Q

Galactose is a C-4 epimer of glucose, which means that it is a?

A

Six carbon aldose.

44
Q

Fructose, galactose. and glucose are all what?

A

Hexose, which means that they are six carbon simple sugars.

45
Q

Fructose differs from glucose and galactose in what ways?

A

Fructose is a 5 carbon (atom) ring where as the galactose and glucose are 6 carbons. Also, glucose and galactose are aldoses (reducing). Fructose is a ketose (non-reducing).

46
Q

One common reason for a reduced Km is?

A

A reduced Vmax. This is given to the fact that Km is 1/2 the Vmax.

47
Q

What are the number of hydrogen donor acceptors and donors when involved in a Watson-Crick base pairing?

A

Adenine: 1 donor and 1 acceptor Thymine: One donor and one acceptor Guanine: 2 donors and one acceptor Cytosine: 2 acceptors and 1 donor. Guanine is generous cytosine is cheap

48
Q

Which three parameters would affect the thrmodynamic stability of the DNA double helix?

A

pH of solution, Ionic strength of solution, and Length of the strand.

49
Q

Which one has larger molecular weight? Adenine or guanine?

A

Guanine. Also larger than deoxy compounds found in DNA duw tho the lack of the 2’ OH group missing on them.

50
Q

The side chain of which amino acid can form a bond that is similar to a peptide bond?

A

Lysine. Because Lysine sidechain can form an isopeptide bond by reacting with a carboxylic group, which is the same way that peptide bonds are formed.

51
Q

Substituting residues in a peptide with which amino acids will result in a peptide with an increase or decreased pI?

A

Lysine is a basic amino acid so it would increase the pI. Glu is an acidic amino acid so it would decrease the pI. Gln and Val are both neutral so they will not affect the pI.

52
Q

Which disacharides are reducing sugars and how many anomeric carbons they have?

A

Maltose (glucose-glucose) is reducing and has one anomeric carbon. Lactose (glucose and galactose) is reducing and has one anomeric carbon. Sucrose (fructose and glucose) is non-reducing and has one anomeric carbon.

53
Q

Phosphate is only able to form what type of bonding?

A

Hydrogen bonding and charge-charge interactions.

54
Q

Side Chain of the aromatic amino acids.

A
55
Q
A