Intro To Protein Structure Flashcards Preview

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Flashcards in Intro To Protein Structure Deck (28)
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1
Q

Nonpolar amino acids

A
Glycine
Alanine
Proline
Valine
Leucine
Isoleucine
2
Q

Aromatic amino acids

A

Phenylalanine
Tyrosine
Tryptophan

3
Q

Polar uncharged amino acids

A

Aspiragine
Glutamine
Serine
Threonine

4
Q

Sulfur-containing amino acids

A

Methionine

Cysteine

5
Q

Charged amino acids

A

Asparate -
Glutamate -

Arginine +
Lysine +
Histidine +

6
Q

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

A

L-form

7
Q

D-form AAs are commonly where?

A

Bacterial cell walls

8
Q

Cysteine residues make up a large part of what protein?

A

Keratin (24%)

9
Q

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

A

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

10
Q

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

A

15, 146

11
Q

Factors that may cause denaturation of proteins

A

Heat, radiation, pH, solvent solution, oxidative damage

12
Q

What are Heinz bodies?

A

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

13
Q

How are Heinz bodies formed?

A

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

14
Q

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

A

Abnormal beta sheets

15
Q

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

A

T

16
Q

Which protein is often the offender in prion diseases?

A

PrP protein

17
Q

The consolidation of beta sheet fibers produces what structures?

A

Amyloid fibers

18
Q

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

A

Congo red (it’s actually yellow)

19
Q

Molecular chaperones work in which two ways?

A
  1. Binding defective proteins to be destroyed with ubiquitin ligase
  2. Binding oligomers to prevent aggregation
20
Q

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

A

Positive cooperative binding

21
Q

Hb subunits can be in one of two states:

A

T (tense)

R (relaxed)

22
Q

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

A

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

23
Q

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

A

F

24
Q

What is the approximate normal HbA1c for nondiabetic adults?

A

~5%

25
Q

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

A

Collagen

26
Q

How many base pairs are abnormal in sickle cell disease?

A

(1) – valine instead of glutamate

27
Q

Sickling of RBCs causes tissue damage in what progression?

A

occlusion–>hypoxia–>necrosis

28
Q

Name a common prion disease

A

Creutzfeldt-Jakob disease