Intro To Protein Structure Flashcards

1
Q

Nonpolar amino acids

A
Glycine
Alanine
Proline
Valine
Leucine
Isoleucine
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2
Q

Aromatic amino acids

A

Phenylalanine
Tyrosine
Tryptophan

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3
Q

Polar uncharged amino acids

A

Aspiragine
Glutamine
Serine
Threonine

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4
Q

Sulfur-containing amino acids

A

Methionine

Cysteine

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5
Q

Charged amino acids

A

Asparate -
Glutamate -

Arginine +
Lysine +
Histidine +

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6
Q

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

A

L-form

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7
Q

D-form AAs are commonly where?

A

Bacterial cell walls

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8
Q

Cysteine residues make up a large part of what protein?

A

Keratin (24%)

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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

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10
Q

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

A

15, 146

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11
Q

Factors that may cause denaturation of proteins

A

Heat, radiation, pH, solvent solution, oxidative damage

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12
Q

What are Heinz bodies?

A

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

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13
Q

How are Heinz bodies formed?

A

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

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14
Q

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

A

Abnormal beta sheets

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15
Q

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

A

T

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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

24
Q

What is the approximate normal HbA1c for nondiabetic adults?

25
Glycocylation of what type of cardiac tissue may result in cardiomyopathy?
Collagen
26
How many base pairs are abnormal in sickle cell disease?
(1) -- valine instead of glutamate
27
Sickling of RBCs causes tissue damage in what progression?
occlusion-->hypoxia-->necrosis
28
Name a common prion disease
Creutzfeldt-Jakob disease