Week 1, Lecture 1: Intro to Protein Structure Flashcards

1
Q

How are peptide bonds formed?

A

amino acids through a condensation reaction to generate the primary sequence

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2
Q

what are weak noncovalent interactions btwn AAs?

A

Hydrophobic interaction, and hydrogen bonds and ionic interactions

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3
Q

what can change the ionization in the R groups, changing enzyme activity?

A

pH, heat

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4
Q

what are Two most common forms of secondary structures?

A

alpha helices and beta-sheet

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5
Q

Describe Myoglobin, type of protein and # of helices…

A

Globular protein, 8

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6
Q

One type secondary structure make what type of protein?

A

Globular (most compactly folded), NOT fibrous

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7
Q

Proteins that have similar folds often have similar…..

A

functions

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8
Q

Myoglobin transports O2 to ____ for storage.

A

mitochondria

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9
Q

Hemoglobin transports O2 from ___ to ___.

A

lungs to tissues

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10
Q

What are some factors that might cause a protein to unfold?

A

Oxidative damage, organic solvents, changes in pH, or changes in temperature can cause proteins to denature

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11
Q

Denaturation exposes hydrophobic residues which can then lead to….?

A

aggregation making the protein insoluble

eg. heinz bodies

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12
Q

Can you name any diseases associated with protein aggregation?

A

Alzheimers, parkinsons, type II diabetes, cancer

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13
Q

what happens in Prion diseases?

A

like Creutzfeldt-Jakob disease, proteins exhibit an increase in beta-sheets.

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14
Q

Whats the result of An increase in beta-sheets?

A

leads to self-association and the formation of amyloid fibers

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15
Q

Molecular chaperones are used by the cell for what?

A

to prevent the aggregation of misfolded proteins

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16
Q

multiple polypeptide chains?

A

quaternary structure

17
Q

hemoglobin has how many alpha and beta chains?

A

[α(2):β(2)]

tetrameric hemeprotein

18
Q

Positive cooperativity results in what shape?

A

sigmoid shaped curve

19
Q

Is an allosteric modulator that promotes T state?

A

2,3-bisphosphoglycerate: at high altitudes

BPG levels increase

20
Q

what kind of posttranslational modifications can alter protein structure and function?

A

carbohydrate addition, lipid addition, regulation

21
Q

what happens when there is a decrease in glycosylation?

A

higher turn over of RBC

22
Q

what is a glycosylated protein called that can for a large protein aggregate?

A

advanced glycation end products

23
Q

Glycosylation of hemoglobin (irreversible) has little effect on function but glycosylation of collagen in the heart results in ???

A

cardiomyopathy

24
Q

Sickle cell anemia can be caused by a point mutation converting ____ to ____? what position? what chain?

A

glutamatic acid to valine at position 6 in β chain resulting in aggregation

25
when is polymerization favorable?
concentration of HbS and is favored when hemoglobin is in the deoxygenated form
26
The polymerization of hemoglobin results in ....?
sickling of the red blood cells and anemia
27
sickling increases ____ of membrane and increasing _____?
Sickling increase permeability of membrane increasing intracellular Ca++
28
Sickling of red blood cells can result in what effects?
occlusion of red blood vessels leading to organ damage and stroke, hypoxia >>> necrosis
29
Sickle cell disease onset occurs at approximately what age?
four months when hemoglobin switching occurs
30
HbF has reduced | Affinity for?
BPG
31
Glu6Val
HbS
32
(α2β2S) sickle cell disease/anemia
HbSS
33
(α2β2A) normal
HbAA
34
sickle cell trait; only 1% of cells sickled
HbSA
35
Glu6Lys
HbC
36
compound heterozygous sickle cell disease
HbSC
37
result from altered ratio of alpha: beta globin
Thalassemias