Exam 2 proteins Flashcards

1
Q

what are the 4 types of globular proteins?

A

all a, all b, a/b, little secondary structure

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2
Q

proteins with little secondary structure function by _____

A

binding with other molecules

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3
Q

what is the most typical globular shape?

A

a/b

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4
Q

___ ____ are amino acid sequences that are used repeatedly in the same protein or are found in different proteins

A

protein domains

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5
Q

protein domains are typically __ to ___ amino acids long

A

40, 100

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6
Q

do protein domains have the same or different function in different proteins?

A

different

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7
Q

what are the two ways that protein domains are formed?

A

duplication of DNA segments within a gene, insertion of a DNA segment into another gene

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8
Q

some domains are ____ and their function is unknown

A

neutral

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9
Q

domains ____ over time and do not resemble the original

A

mutate

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10
Q

what is the first step of protein folding?

A

new polypeptide forms segments of secondary structure, either a helix or beta sheets

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11
Q

a helix and b sheet formation is due to what type of bonding?

A

hydrogen

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12
Q

what is the second step of protein folding?

A

secondary structures form a globular shape

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13
Q

how is a globular shape aquired?

A

through hydrophobic interactions

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14
Q

what is the third step of protein folding?

A

tertiary structure is generated by adjustments to the folded structure

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15
Q

____ ____ are proteins in the cell that bind new proteins and help bring parts together to get the proper 3D folding

A

molecular chaperones

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16
Q

the intermediates of protein folding involve __-___ __ ___

A

R-side chain interactions

17
Q

____ ____ are misfolded, insoluble and aggregated proteins in brain cells

A

amyloid deposits

18
Q

what protein is misfolded in Alzheimer’s Disease?

A

amyloid-b

19
Q

what protein is misfolded in Parkinson’s Disease?

A

s synuclein

20
Q

___ and ____ are produced via the same type of forces

A

tertiary, quaternary

21
Q

quaternary structure allows for __ ____ between subunits of proteins

A

cooperative behavior

22
Q

how does hemoglobin exhibit cooperative behavior?

A

the binding of the first O2 molecule makes it easier for the 3 other O2 molecules to each bind to a subunit

23
Q

nitrite reductase, fumarase, hemoglobin, and methane hydroxylase all have what type of quaternary structure?

A

fixed number of subunits

24
Q

microtubules have what type of quaternary structure?

A

open

25
Q

___ ___ polymerize to form microtubules

A

tubulin dimers

26
Q

folding of a newly synthesized protein into the final 3D structure primarily involves the interactions of what?

A

amino acid side chains

27
Q

a protein has quaternary structure if it has more than ____ polypeptide chain

A

1

28
Q

_____ primarily hold together tertiary and quaternary structure

A

hydrophobic

29
Q

what 3 things hold together tertiary and quaternary structure?

A

hydrophobic interactions, hydrogen bonds, and ionic interactions

30
Q

____ ______ are when the interacting surfaces are identical and the resulting structure is dimeric

A

isologous interactions

31
Q

____ ______ involve nonidentical interfaces, and the surfaces must be complementary

A

heterologous associations

32
Q

reducing the protein’s surface to volume ratio increases its ____

A

stability

33
Q

what are the 4 benefits of quaternary association?

A

stability, genetic economy/efficiency, catalytic sites coming together, cooperativity