Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Biochemistry > Protein Structure > Flashcards

Protein Structure Flashcards

1
Q

The only form of protein structure not affected by denaturation?

A

Primary Structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

States that at least for a small globular protein in its standard physiological environment, the native structure is determined only by the protein’s amino acid sequence

A

Anfinsin’s Dogma

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

A paradox that arises since the native folded state of protein by a random search among all possible configurations can take an enormously long time yet proteins can fold in seconds or less.

A

Levinthal Paraxox

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

True or False. Most of the amino acids are a-amino acids

A

True. It means both amino and carboxyl groups are attached to the a carbon atom.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What amino acids has the largest side chain?

A

Tryptophan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Identify the branched-chain amino acids whose metabolites accumulate in MSUD

A
  1. Leucine
  2. Isoleucine
  3. Valine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is considered to be the 21st amino acid?

A

Selenocysteine (Sec)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Considered the 22nd Amino Acid

A

Pyrrolysine (Pyl)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What are the essential amino acids ?

A
  1. Phenylalanine
  2. Valine
  3. Threonine
  4. Tryptophan
  5. Isoleucine
  6. Methionine
  7. Histidine
  8. Arginine
  9. Lysine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

This is the only semi-essential amino acid

A

Arginine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Characteristic of a peptide bond

A

Has a partial double-bond character

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Angle between the alpha carbon and the nitrogen

A

Phi Angle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Angle between the alpha carbon and the carbonyl carbon

A

Psi angle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

This terminus contains targeting signals, that targets protein to a specific organelle

A

N-terminus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

This terminus has retention signals for protein sorting , which keeps the protein in the endoplasmic reticulum

A

C-terminus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Part of a polypeptide that consist of a free -COOH structure

A

C-terminal

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Which is the terminal ends of proteins that can be modified post translationally , most commonly by the addition of a lipid anchor that allows the protein to be inserted into a membrane without having transmembrane domain?

A

C-terminal

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What do you call the supersecondary structures produced by packing side chains from adjacent secondary structural elements close to each other?

A

Motifs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What is the fundamental functional and three-dimensional structural units of polypeptide called?

A

Domains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

These are specialized group of proteins required for the proper folding of many species of proteins

A

Chaperones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Porphyrins have a maximum characteristic electronic absorption spectrum around _________ nm known as the Sorek peak.

A

400nm

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Factors that cause the hemoglobin curve to shift to the right.

A
  1. CO2 ⬆️
  2. Acidity ⬆️ (⬇️pH)
  3. 2,3-BPG ⬆️
  4. Exercise ⬆️
  5. Temperature ⬆️
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

When blood glucose enters the erythrocytes, it glycates which amino acid?

A

Lysine : Inc glycation of hgb noted in px with dm due to inc glucose in the blood

24
Q

Hydroxylation of proline and lysine residues require which vitamin?

A

Vitamin C

25
Q

Identify the most common type of Ehlers- Danlos syndrome

A

Hypermobility, other subtypes include classical and vascular.

26
Q

This refers to the part of the antigen to which antibody binds

A

Epitope

27
Q

This refers to the part of the antigen to which an antibody binds to the epitope of the antigen

A

Paratope

28
Q

This class of enzyme cleaves substrate bonds using water (adding H+ or OH-) to the cleavage products.

A

Hydrolases

29
Q

This class of enzyme catalyzes cleavage of C-C, C-S, and certain C-N bonds

A

Lyases

30
Q

This class of enzyme catalyzes the formation of bonds between C and O, S, and N coupled to hydrolysis of high energy phosphates

A

Ligases (g for group)

31
Q

This refers to the active enzyme + nonprotein component .

A

Holoenzyme

32
Q

This refers to the enzyme without its nonprotein component

A

Apoenzyme

33
Q

This refers to the nonprotein component that is a metal ion

A

Cofactor

34
Q

This refers to the nonprotein component that is small and organic molecule

A

Coenzyme

35
Q

True or False. Coenzymes are usually derived from minerals.

A

False, coenzymes are usually derived from vitamins.

36
Q

Characteristic of a competitive inhibitor.

A

Increases apparent Km without affecting Vmax

37
Q

Identify the type of enzymes that is regulated by molecules called effectors that bind noncovalently at a site other than the active site.

A

Allosteric Enzymes

38
Q

Thyroid hormones production from thyroid glands

A
  1. Thyroxine (T4): 80-90%
  2. Triiodothyronine (T3): 10-20%
39
Q

Identify the endopeptidases specific of the sites of basic AAs

A

Trypsin

40
Q

Identify the endopeptidases specific at sites of neutral AAs

A
  1. Chymotrypsin
  2. Elastase
41
Q

Identify the ectopeptidase specific at neutral AA at C- terminus

A

Carboxypeptidase A

42
Q

Characteristic of binding of Oxygen by Hgb.

A

The O2 affinity of Hgb increases as the percentage saturation increases

43
Q

The Oxyhemoglobin dissociation curve relates the ______ of oxygen in the blood to the _____ of hemoglobin with oxygen

A

Partial pressure; Percent saturation

44
Q

Increases in CO2 levels lowers the pH of blood causing hemoglobin to release O2 to the body tissues. What is this phenomenon?

A

Bohr Effect

45
Q

Removal of O2 from hemoglobin causes increase in affinity of hemoglobin for CO2 , allowing it to be expired into the lungs. What is this phenomenon?

A

Haldane Effect

46
Q

This describes the exchange of bicarbonate and chloride across the membrane of the RBCs.

A

Chloride shift or Hamburger Effect

47
Q

Each 1g of hemoglobin can maximally bind _____ ml of O2.

A

1.34mL

48
Q

Any of these genes are mutated in Alport Syndrome

A

Type IV collagen genes (heterotrimers)
1. COL4A3
2. COL4A4
3. COL4A5

49
Q

What are the hormones secreted by the anterior pituitary?

A
  1. TSH
  2. FSH
  3. LH
  4. ACTH
  5. GH
  6. Prolactin
    (FLAG PT)
50
Q

Which has a higher O2 affinity?
Adult Hgb or Fetal Hgb?

A

Fetal Hgb

51
Q

Are enzymes nutritionally essential?

A

No

52
Q

What amino acid is a major excitatory neurotransmitter?

A

Glutamate

53
Q

What amino acid is a major inhibitory neurotransmitter?

A

Glycine

54
Q

What amino acid is biosynthetic precursor to porphyrins in red blood cells ?

A

Glycine

55
Q

What amino acid is most abundant in collagen ?

A

Glycine

56
Q

What amino acid is used in lipid transport?

A

Lysine

57
Q

Aspartame is composed of what amino acids? (3)

A

Phenylalanine
Methanol
Aspartic acid

Biochemistry (19 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions