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
Q

when is polymerization favorable?

A

concentration of HbS and is favored when hemoglobin is in the deoxygenated form

26
Q

The polymerization of hemoglobin results in ….?

A

sickling of the red blood cells and anemia

27
Q

sickling increases ____ of membrane and increasing _____?

A

Sickling increase permeability of membrane increasing intracellular Ca++

28
Q

Sickling of red blood cells can result in what effects?

A

occlusion of red blood vessels leading to organ damage and stroke, hypoxia&raquo_space;> necrosis

29
Q

Sickle cell disease onset occurs at approximately what age?

A

four months when hemoglobin switching occurs

30
Q

HbF has reduced

Affinity for?

A

BPG

31
Q

Glu6Val

A

HbS

32
Q

(α2β2S) sickle cell disease/anemia

A

HbSS

33
Q

(α2β2A) normal

A

HbAA

34
Q

sickle cell trait; only 1% of cells sickled

A

HbSA

35
Q

Glu6Lys

A

HbC

36
Q

compound heterozygous sickle cell disease

A

HbSC

37
Q

result from altered ratio of alpha: beta globin

A

Thalassemias