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BIOL 231 > Week 7_levels of protein structure > Flashcards

Week 7_levels of protein structure Flashcards

1
Q

describe the amino acid structure

A

central carbon

amino terminal end

carboxyl terminal end

R group

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2
Q

what is an R group?

A

variable part of amino acids

give amino acids their individual electrochemical characteristics

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3
Q

how many levels of protein structure are there?

A

4

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4
Q

what is primary structure?

A

sequence of amino acids in a protein

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5
Q

are R groups part of the peptide backbone?

A

no

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6
Q

what is secondary structure in a protein?

A

folding of the protein that is caused by interactions w/in the peptide backone

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7
Q

where do hydrogen bonds form in secondary structure?

A

form b/n amino hydrogen and carboxyl oxygen atoms

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8
Q

what type of secondary structures are there in proteins?

A

alpha-helix

beta-pleated sheets (consist of 2 or more hydrogen bonded B-strands)

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9
Q

what is a super secondary structure?

A

forms when alpha-helices and beta-pleated sheets combine in various ways to form motifs

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10
Q

what are examples of super secondary structures?

A

B-barrel

B-a-B-unit

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11
Q

what type of bonding holds secondary structures together within the peptide backbone?

A

H-bonding

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12
Q

what is the tertiary structure?

A

the entire 3D structure of the entire folded protein

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13
Q

tertiary structure is stabilized by interactions between…

A

R groups of the amino acids

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14
Q

what are the types of R group interactions?

A

electrostatic interactions
- H bonding
- ionic bonding

disulfide bridges

Van der Waals interactions

hydrophobic interactions

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15
Q

what are electrostatic interactions?

A

form b/n R groups to help stabilize tertiary structure

hydrogen bonds b/n R groups

ionic bonds b/n R groups

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16
Q

what are disulfide bridges?

A

form b/n R groups to help stabilize tertiary structure

cysteines have a sulfhydryl (SH) group

the SH groups of 2 cysteine residues can form covalent bonds called disulfide (S-S) bridges

17
Q

what are Van Der Waals interactions

A

help stabilize tertiary structure

a weak attractive force b/n non polar molecules due to charge fluctuations in the electron clouds of atoms

18
Q

what are hydrophobic interactions?

A

hydrophobic (water-fearing) R groups will fold to the interior of the protein to avoid contact with aqueous environment

19
Q

what are protein domains?

A

functional subunits of a protein

20
Q

how are protein domains formed?

A

from a combination of secondary and tertiary interactions

21
Q

one protein can form multiple ___

A

domains

22
Q

any protein that directly binds to DNA (ex. transcription factors) needs a ___

A

DNA binding domain

23
Q

activating transcription of gene requires a ___ to recruit ___

A

transcriptional activation domain (TAD)

RNA polymerase

24
Q

what is the highest level of structure for a single protein?

A

tertiary structure

25
Q

what is quaternary structure?

A

the interaction of multiple proteins into multi-protein complexes

26
Q

what is an example of quaternary structure?

A

hemoglobin protein in RBC’s

27
Q

what does a hemoglobin consist of?

A

2 alpha and 2 beta proteins

(4 proteins = tetramer)

28
Q

what does hemoglobin do?

A

carries oxygen from lungs to cells of body

29
Q

proper folding is critical to ___

A

protein function

30
Q

what are chaperone proteins?

A

enzymes that help proteins fold and/or refold

provide an optimal folding environment for other proteins

31
Q

chaperones are critical to the proper ___ and ___ of most proteins

A

folding

refolding

32
Q

___ are unable to function properly and are the cause of certain diseases

A

misfolded proteins

33
Q

what is cystic fibrosis?

A

disease in which abnormally thick mucus blocks airways, causing difficulty breathing

34
Q

what does the CFTR protein do?

A

regulates the thickness of mucus

35
Q

what does a mutation in the CFTR gene do?

A

blocks the interaction b/n the CFTR protein and its chaperone protein

CFTR protein cannot fold properly and is unable to function

36
Q

describe relationship between Alzheimer’s disease and protein folding

A

misfolded Tau proteins and beta-amyloid proteins form protein clumps (tangles and plaques) that collect inside and outside of neurons in the brain and destroy them

37
Q

protein misfolding is believed to be the primary cause of:

A
  • PD
  • HD
  • CJD
  • many other degenerative and neurodegenerative disorders
38
Q

therapeutic strategies to reverse ___ or introduce ___ versions of the proteins are an active area of research

A

reverse misfolding

introduce properly folded versions

BIOL 231 (23 decks)

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