Module 2 Flashcards

(30 cards)

1
Q

How to build a macromolecule?

A

Condensation reactions, remove water

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2
Q

How to break up a biopolymer?

A

Hydrolysis reactions, add water

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3
Q

How are proteins linked and what do they form?

A

linked by amide linkages to form peptide bonds

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4
Q

How to make up proteins?

A

Bunch of amino acids

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5
Q

Is the backbone of a peptide bond hydrophilic or hydrophobic?

A

hydrophilic

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6
Q

Which direction do you read a protein? (C/N terminis)

A

Read from positive amino (N) to negative carboxy (C)

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7
Q

What is primary structure?

A

linear sequence of amino acids

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8
Q

What is secondary structure?

A

regularly repeating folding patterns

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8
Q

What is tertiary structure?

A

overall three dimensional fold

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9
Q

What is quaternary structure?

A

assembly of subunits

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10
Q

What does aliphatic mean?

A

side chains made up of just carbon and hydrogen

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11
Q

What is phosphorylation and what amino acids are impacted?

A

hydroxyl replaced by phosphate group
ex: tyrosine kinases
Impacts: Ser, Thr, Tyr

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12
Q

What is hydroxylation and which amino acids are impacted?

A

Stabilization of structures
Ex: Collagen
Impacts: Pro, Lys

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13
Q

What is methylation and which amino acids are impacted?

A

Cell marker
Examples: Histones
Impacts: Lys, Arg, His

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14
Q

What is ubiquitination?

A

a protein can be modified through a chemical linkage to a second protein called ubiquitin
occurs at a lysine residue

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15
Q

How are secondary structures primarily stabilized?

A

hydrogen bonding

16
Q

What are the phi and psi angles?

A

phi: C-N
psi: C-C

17
Q

What is the structure of alpha helicies?

A

extensive hydrogen bonding between residues n and n+4
core is tightly packed to protect the hydrogen bonding

18
Q

What is the difference in spacing (in angstroms) between alpha helices and beta sheets?

A

1.5 angstroms vs 3.5 angstroms between residues

19
Q

What are the two types of beta sheets and which is more stable?

A

antiparallel (opposite N-C direction) and parallel (same N-C direction)
antiparallel is more stable because the H-bonding is linear

20
Q

In terms of a Ramachandran plot, which amino acid is most and least sterically hindered?

A

Proline is the most sterically hindered because of the proline ring, and glycine is the least sterically hindered

21
Q

In terms of a Ramachandran plot, which secondary structure has more possibilities?

A

Beta sheets have higher possibilities because it is spread out compared to the specific H-Bonding that needs to occur for an alpha helix

22
Q

What are reverse turns for and where are they found?

A

used to turn a protein 180 degrees, found on the protein surface
n and n + 3

23
Q

What is the differences between a Type I and II reverse turn?

A

Type I: carbonyl and R group are facing away
Type II: carbonyl and R group are facing the same side (usually forcing the R group to be Glycine)

24
What is the purpose of a 3(10) helix?
cap off alpha helices, very sharp turns R group usually proline
25
What is the key differences with polyproline helix?
stabilized by van der waals instead of hydrogen bonds Ex: collagen Repeating sequences of Gly-Pro-Hydroxy Forms a triple helix
26
What are supersecondary structures?
Beta-Alpha-Beta sheets Beta hairpin alpha alpha motif
27
What are tertiary structures?
gives overall protein fold and shape determined by linear sequence of amino acids
28
What are domains?
Proteins often contain discrete units Folded, structurally independent regions
29
What is quaternary structure?
arrangement of individual subunits with respect to each other Subunits often linked by non-covalent forces