Pearls from AAMC Material/ Khan Academy/ Practice Exams Flashcards

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1
Q

What is a phosphatase?

A

an enzyme that removes a phosphate group from its substrate

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2
Q

We know that anions such as formate and urate (ending in -ate) are….

A

…anions that can accept protons.

(https://www.khanacademy.org/test-prep/mcat/physical-sciences-practice/physical-sciences-practice-tut/e/biochemistry-changes-that-occur-after-death?_ga=2.94837077.819408990.1653668529-826931683.1648912754)

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3
Q

When the pH of the solution is greater than the pKa for a proton, the proton is removed and the compound becomes ____________ at that region.

A

deprotonated

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4
Q

What does fructose-2,6-bisphosphate do?

A

It stimulates phosphofructokinase (PFK), and inhibits fructose-1,6-bisphosphatase

(Princeton Review practice Exam 1)

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5
Q

Peptidoglycans are not found in eukaryotes, only ________.

A

bacteria

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6
Q

All 20 amino acids are primary amines except for ______, which has its N atom in a five-membered ring, making it a secondary amine.

A

proline

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7
Q

Which blotting test is used for detection of a protein?

A

Western blotting

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8
Q

Which test is used for detection of specific RNA sequences?

A

Northern blot

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9
Q

Which test is used for detection of specific DNA sequences?

A

Southern blot

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10
Q

Both column chromatography and thin-layer chromatography separate compounds based on ________, while gas chromatography separates compounds based on ______ ______.

A

polarity

boiling points

(Khan Academy passage: Separations and purifications)

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11
Q

In thin layer chromatography, which uses a polar silica gel for the stationary phase, which substance will elute first?

A

the non-polar substance will elute first, because it travels with the nonpolar mobile phase

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12
Q

In size-exchange chromatography, substances are sorted based on their molecular weight. Which substance elute first? Which elute last?

A

Larger molecules will elute first
smaller molecules elute last bc they have a longer path to travel.

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13
Q

In CATION-Exchange Chromatography, the Stationary Phase (charged beads) is negatively charged; Thus, _______ will be retained in the column.

In ANION-Exchange Chromatography, the Stationary Phase is positively charged. Thus, ______ will be retained in the column.

Remember, this type of analysis is named after the END GOAL, which is to get cations to stick in the column.

A

CATIONS

ANIONS

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14
Q

Where is rRNA synthesized?

A

in the nucleolus

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15
Q

Some RNAs have more than 4 different types of bases. What is an example of this?

A

tRNA has unique and modified bases apart from the traditional four bases A,U,C, and G (such as inosine, methylinosine, and several others)

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16
Q

Which 2 amino acids are known as ALPHA HELIX breakers?

A

glycine (bc its so flexible)
proline (bc it has a secondary alpha amino group)

(Khan Academy video: Special Cases: Histidine, proline, glycine, cysteine)

17
Q

Which types of protein structure are affected by heat?

A

Heat can destroy 2°, 3°, and 4° protein structure but leaves 1° structure intact.

(Khan Academy video)

18
Q

An acid, like vinegar disrupts what levels of protein structure?

A

An acid will disrupt 3° and 4° structure, because it affects ionic bonds.

19
Q

What level of protein structure are enzymes capable of destroying?

A

Primary structure can be disrupted by enzymes, which would essentially destroy all levels of protein structure.

20
Q

A ______ adds on a phosphate group to a molecule by removing a hydrogen and creating a bond between the oxygen of the hydroxy group and the phosphate of the phosphate group (O-P).

A

kinase

An amino cannot be phosphorylated by a kinase if it lacks a hydroxyl group.
(unsure if the basic and acidic amino acids can be phosphorylated but I think so; alkyl side chains cannot be phosphorylated)

21
Q

Things to know about SDS-page electrophoresis:

A

This requires the disruption of the native conformations of the proteins of interest.

It is not carried out under physiological conditions (BME and SDS are not present in living systems).

It uses a voltage gradient to spatially separate electrically charged proteins.

It is carried out in a pH buffered solution to ensure that the proteins being separated maintain the desired electrical charge.

22
Q

SDS is used to ensure that polypeptides have a ________ ______ proportional to the length of the molecule.

A

negative charge

https://www.khanacademy.org/test-prep/mcat/biological-sciences-practice/x04f6bc56:mcat-bio-biochem-foundation-1-passages/e/the-electrophoretic-separation-of-proteins

23
Q

Prions cause misfolding of proteins which aggregate and cause disease. One well-known mechanism by which this happens is when ______ _-_______ are replaced by β-sheets. The β-sheets have a higher likelihood of binding to one another, and this causes aggregation of proteins.

A

normal α-helices

(MCAT Self Prep End-of-Lesson cards)

24
Q

β-turns are sharp turns in the amino acid sequence that allow proteins to maintain a compact structure. They are normally located on the _______ of proteins.

A

SURFACE

(End-of-lesson mastery questions)

25
Q

The secondary structure of keratin is largely composed of α-helices. The majority of these are _____-______ (clockwise) in order to decrease steric hindrance.

A

right-handed

(End-of-lesson mastery quiz)

26
Q

Vitamin B3 (niacin) is a precursor for….

A

….NAD.

27
Q

Vitamin B5 (pantothenic acid), is a precursor for…

A

….CoA.

28
Q

Consider the transport of proteins that need to be modified. The usual process to produce these proteins follows these steps: cytoplasm -> endoplasmic reticulum -> Golgi apparatus -> cell membrane. If some molecule aided in RETROGRADE transport from the Golgi apparatus, it would follow the reverse of this path.

A
29
Q

Do archaea and bacteria have a Golgi apparatus?

A

No

30
Q

If the concentration of amino acid transport protein is increased, the transport affinity Kt of L-alanine will:

A

not change!

Transport affinity for substrates (in this case, alanine) is an inherent property of transport proteins, and thus transport affinity is independent of the concentration of transport protein.

[AAMC Free Practice Exam]

31
Q

In standard Michaelis–Menten kinetics, Kt is equal to:

A

For transporters the transport affinity (Kt) is equivalent to the KM in Michaelis–Menten kinetics. This means that Kt is the substrate concentration at which the reaction rate is one-half the maximal transport capacity.

[AAMC Free Practice Exam/ Bio/Biochem section, Q 25]

32
Q

The metabolic rate is an internal variable that will help define the capability of an organism to withstand long periods of ________ deprivation. An organism that has a low metabolic rate will be more suitable to withstand long periods of food deprivation than an organism that has a high metabolic rate.

A

nutrient

[AAMC Free Practice Exam/ Bio/Biochem section]

33
Q

What is the “anatomy” of a fatty acid?

A

a carboxyl group “head” (CO2-) with a hydrocarbon tail

34
Q

The smaller the Kd, the _______ the binding affinity of the ligand for its target.

A

GREATER

[Q 55 of AAMC Free Practice Exam]

35
Q

The passage indicates that subunit A of STx protein is a polypeptide chain that is cleaved. The cleavage of peptide bonds is catalyzed by a ________.

A

protease

36
Q

When Leu, a hydrophobic amino acid, is located at a surface-exposed site of proteins, it is in contact with water molecules and, therefore, water molecules must organize themselves into a specific arrangement (called _______ _______) to live with this fact. A substitution of Leu to Thr, which is a polar and hydrophilic amino acid, reduces drastically this entropic penalty because water molecules are now in contact with a hydrophic amino acid.

A

entropic penalty