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38 Terms

1
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with gel electrophoresis, which side has the anode, and which side has the cathode

anode is to the right, cathode is to the left

2
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hydrophobic effects drives what level of protein structure formation?

tertiary structure

3
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if pH>pI, does the protein gain (-) or lose (-) electrons?

loses protons, becomes deprotonated

4
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if pH<pI, does the protein gain (-) or lose (-) electrons?

gains protons, becomes protonated

5
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what is pI?

pH when protein’s charge is neutral

6
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are integrated membrane proteins hydrophobic or hydrophilic?

hydrophobic

7
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does phosphorylation cause a molecule to become more positive or negative?

more negative

8
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does dephosphorylation cause a molecule to become more positive or negative?

more positive

9
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are D- or L- amino acids more uncommon in nature?

D-amino acids

10
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are D- or L- amino acids more recognized by proteases?

L-amino acids

11
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do enantiomers have the same charge?

yes

12
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amino acids with thiols (-SH) and hydroxyls (-OH) act as _____ in biological reactions

nucleophiles

13
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when amino acids with thiols and hydroxyls are deprotonated, it _______ their nucleophilicity

betters

14
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what is salt bridging?

when elements of H-bonding and ionic bonding are combined (occurs between oppositely charged molecules); leads to electrostatic interactions

15
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between which amino acids does salt bridging occur?

aspartic acid or glutamic acid, and lysine or arginine

16
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what are proteases?

enzyme that catalyzes hydrolysis of peptide bonds in polypeptide chains

17
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why are proteases’ movement limited?

since the double bond can switch positions (between O and N)

18
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what are G proteins?

signaling proteins in cells that are switched “on” a when they bind to GTP, and “off” after GTP is hydrolyzed (GTP—>GDP, where bonds are broken)

19
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is glycine chiral or achiral?

achiral

20
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is cysteine chiral or achiral?

chiral

21
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does cysteine have (S)- or (R)- configuration?

(R)-configuration

22
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is cysteine a D- or L- amino acid?

L-amino acid

23
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when pH>pka, _____ form decreases, and _____ form increases

protonated, deprotonated

24
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when pH<pka, _____ form decreases, and _____ form increases

deprotonated, protonated

25
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why does tryptophan like fluorescence?

because of its conjugation

26
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why is proline unique?

because it possesses a secondary amino (imine) group, which can help position neighboring atoms

27
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which two amino acids are exclusively found at beta turns?

proline and glycine (other a.a’s are found at a-helices)

28
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if it’s a hydrophilic molecule (i.e. peptide hormones), does it require a second messenger?

yes

29
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if it’s a hydrophobic molecule (i.e. steroids), does it require a second messenger?

no

30
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what does in vivo mean?

conducted in a living organism

31
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what does in vitro mean?

conducted in a lab

32
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what is a voltage-gated ion channel?

a channel that activates upon a change in membrane potential; usually caused by another ion channel

33
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(forming) peptide bonds are thermodynamically _____ and kinetically _____

unstable (because it requires GTP hydrolysis/energy input), stable (because it has a high activation energy, meaning it’ a slow reaction)

34
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which proteins migrate the fastest/slowest in SDS-PAGE?

smaller proteins migrate fastest, larger proteins migrate slowest

35
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which proteins migrate the fastest/slowest in size exclusion chromatography?

larger proteins migrate fastest, smaller proteins migrate slowest

36
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what do reducing agents do in SDS-PAGE/size exclusion chromatography?

break the bonds in between dimers, etc.

37
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what is Western blot?

a protein separation and identification technique by using antibodies to detect specific proteins

38
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what are the steps of Western blot?

  1. protein electrophoresis: separates proteins based on size

  2. protein transfer: transferred from gel —> membrane (blotting)

  3. addition of blocking protein from milk/BSA: prevents non-specific binding of antibodies to membrane

  4. addition of primary antibodies: specifically binds to protein of interest

  5. addition of secondary antibodies: binds to primary antibody and is labeled with a marker for visualization

  6. visualization: using fluorescence/chemiluminescence/autoradiography to visualize; shows up as a band on membrane