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Basic Medical Biochemistry > Peptides and Proteins > Flashcards

Peptides and Proteins Flashcards

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USMLE® Step 1 flashcards
1
Q

What is Ehlers-Danlos Syndrome?

A

Defect in structure, production, or process of collagen or proteins interacting with collagen

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2
Q

Polypeptide chains are what?

Hint: shape

A

Planar

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3
Q

What are amino acids joined covalently by in a peptide chain?

A

Amide bonds

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4
Q

What are proteins also known as?

A

Polypeptides

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5
Q

Proteins have a _____ backbone of _____ different side chains protruding.

A

Repeating; 20

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6
Q

What is the order of chemical interactions that stabilizes a polypeptide?

A

Covalent bond > Disulfide bond > Salt bridge > Hydrogen bond > Van der waals

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7
Q

What happens during a secondary structure?

A

Polypeptides begin to fold

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8
Q

In a secondary structure, hydrogen bonding occurs every ____ amino acids.

A

4

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9
Q

What is the primary stabilizing feature for polypeptides in a secondary structure?

A

Hydrogen bonds

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10
Q

An alpha helix is a what kind of turn?

A

Right hand

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11
Q

Beta strand makes up what?

A

Beta sheets

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12
Q

A beta strand has alternating ____?

A

R groups

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13
Q

In an antiparallel BETA sheet, the adjacent B tuns in what direction?

A

Opposite

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14
Q

What groups connect each amino acid to a single amino acid on adjacent strands?

A

NH and CO groups

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15
Q

In a parallel BETA sheet, the adjacent b runs in what direction?

A

Same

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16
Q

In a BETA sheet, the side chains are located where?

A

Above and below the plane

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17
Q

In a tertiary structure, hydrophobic amino acids are found where?

A

On the inside

18
Q

What are found on the protein surface of a tertiary structure?

A

Charged amino acids (hydrophilic amino acids)

19
Q

Primary structures have what kind of backbone?

A

Linear

20
Q

Secondary structures can consist of what?

A

Alpha helix, Beta sheets, reverse turns

21
Q

What is involved inside a tertiary structure?

Hint: DHH

A

Disulfide bonds, hydrogen bonding, hydrophobic interactions

22
Q

In protein denaturation, OIL is what?

A

Oxidation losing e-

23
Q

In protein denaturation, RIG is what?

A

Reduction is gaining e-

24
Q

What is B-mercaptoethanol?

A
  1. reducing agent that gains H

2. breaks disulfide bonds

25
Q

8m urea is what kind of substance?

A

Harsh substance to denature

26
Q

A native ribonuclease is what kind of structure?

A

Tertiary structure

27
Q

A denatured reduced ribonuclease is what kind of structure?

A

Primary structure

28
Q

In amino acid detection, Trp + Tyrosine = _____ when subjected to UV spec?

A

280nm

29
Q

What is used for sequencing a peptide?

A

Edman degradation allows sequencing of a peptide

30
Q

To study a primary structure, what can be used?

A

Mass spectroscopy, Proteases, Edman degradation

31
Q

When studying a secondary structure, what can be used?

A

Circular dichroism (CD) spectroscopy

32
Q

What does a CD spectroscopy do?

A

Depolarizes light substances depending on secondary structure

33
Q

What can be used when studying a tertiary structure?

A

X-ray crystallography

34
Q

What is the strongest type of chemical reaction that stabilizes a protein?

A

Covalent bond

35
Q

What is the weakest type of chemical interaction that stabilizes a peptide?

A

Van der Waals interaction

36
Q

What two things denature a ribonuclease?

A

8 M Urea and B-mercaptoethanol

37
Q

Which procedure reveals the entire sequence of a peptide?

A

Edman degradation

38
Q

With Edman degradation, what can be released without hydrolyzing the rest of the peptide?

A

Amino-terminal residue

39
Q

Trypsin cleaves at the carboxyl end of what amino acids?

A

Arginine and lysine

40
Q

Chymotrypsin cleaves at the carboxyl end of what amino acids?
Hint: PTT

A

Phenylalanine, tyrosine, tryptophan

41
Q

CNBR cleaves at the end of what amino acid?

A

Methionine

42
Q

Denaturation can cause the loss of what structures due to unfolding of the polypeptide chain?

A

Secondary, tertiary, and quaternary

Basic Medical Biochemistry (3 decks)

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