Intro To Protein Structure

Question 1

Nonpolar amino acids

Answer 1

Glycine
Alanine
Proline
Valine
Leucine
Isoleucine

Question 2

Aromatic amino acids

Answer 2

Phenylalanine
Tyrosine
Tryptophan

Question 3

Polar uncharged amino acids

Answer 3

Aspiragine
Glutamine
Serine
Threonine

Question 4

Sulfur-containing amino acids

Answer 4

Methionine

Cysteine

Question 5

Charged amino acids

Answer 5

Asparate -
Glutamate -

Arginine +
Lysine +
Histidine +

Question 6

AAs with which chirality type are found predominantly in human proteins?

Answer 6

L-form

Question 7

D-form AAs are commonly where?

Answer 7

Bacterial cell walls

Question 8

Cysteine residues make up a large part of what protein?

Answer 8

Keratin (24%)

Question 9

Explain how an alpha-helix can contain AAs with both polar and nonpolar side chains

Answer 9

The polar side chains can face into the aqueous environment on one side while the nonpolar side chains face into a nonpolar environment on the opposite side

Question 10

Only ____ residues out of ____ are identical in myoglobin and hemoglobin

Answer 10

15, 146

Question 11

Factors that may cause denaturation of proteins

Answer 11

Heat, radiation, pH, solvent solution, oxidative damage

Question 12

What are Heinz bodies?

Answer 12

Protein aggregations resulting from the exposure and aggregation of proteins, making them insoluble

Question 13

How are Heinz bodies formed?

Answer 13

Oxidative damage–>oxidative O2 species–>Hb denaturation–>protein aggregates–>hemolysis–>anemia

Question 14

Prion diseases are characterized by the abnormal folding of proteins in what way?

Answer 14

Abnormal beta sheets

Question 15

T/F Prion diseased proteins maintain the same primary structure as nondiseased proteins

Answer 15

T

Question 16

Which protein is often the offender in prion diseases?

Answer 16

PrP protein

Question 17

The consolidation of beta sheet fibers produces what structures?

Answer 17

Amyloid fibers

Question 18

What type of stain is used to identify prion diseases pathologically?

Answer 18

Congo red (it’s actually yellow)

Question 19

Molecular chaperones work in which two ways?

Answer 19

1. Binding defective proteins to be destroyed with ubiquitin ligase
2. Binding oligomers to prevent aggregation

Question 20

Hb binds each subsequent oxygen molecule with more affinity than the previous. This is known as

Answer 20

Positive cooperative binding

Question 21

Hb subunits can be in one of two states:

Answer 21

T (tense)

R (relaxed)

Question 22

This compound promotes salt bridge formation between Hb subunits and decreases oxygen binding to Hb

Answer 22

2,3-BPG (2,3-bisphosphoglyerate)

Question 23

T/F The glycosylation of Hb is a nonenzymatic, reversible reaction

Answer 23

F

Question 24

What is the approximate normal HbA1c for nondiabetic adults?

Answer 24

~5%

Question 25

Glycocylation of what type of cardiac tissue may result in cardiomyopathy?

Answer 25

Collagen

Question 26

How many base pairs are abnormal in sickle cell disease?

Answer 26

(1) – valine instead of glutamate

Question 27

Sickling of RBCs causes tissue damage in what progression?

Answer 27

occlusion–>hypoxia–>necrosis

Question 28

Name a common prion disease

Answer 28

Creutzfeldt-Jakob disease