Intro To Protein Structure Flashcards Preview

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

Nonpolar amino acids

Glycine
Alanine
Proline
Valine
Leucine
Isoleucine

2

Aromatic amino acids

Phenylalanine
Tyrosine
Tryptophan

3

Polar uncharged amino acids

Aspiragine
Glutamine
Serine
Threonine

4

Sulfur-containing amino acids

Methionine
Cysteine

5

Charged amino acids

Asparate -
Glutamate -

Arginine +
Lysine +
Histidine +

6

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

L-form

7

D-form AAs are commonly where?

Bacterial cell walls

8

Cysteine residues make up a large part of what protein?

Keratin (24%)

9

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

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

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

15, 146

11

Factors that may cause denaturation of proteins

Heat, radiation, pH, solvent solution, oxidative damage

12

What are Heinz bodies?

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

13

How are Heinz bodies formed?

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

14

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

Abnormal beta sheets

15

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

T

16

Which protein is often the offender in prion diseases?

PrP protein

17

The consolidation of beta sheet fibers produces what structures?

Amyloid fibers

18

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

Congo red (it's actually yellow)

19

Molecular chaperones work in which two ways?

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

20

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

Positive cooperative binding

21

Hb subunits can be in one of two states:

T (tense)
R (relaxed)

22

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

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

23

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

F

24

What is the approximate normal HbA1c for nondiabetic adults?

~5%

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