Biomolecules - Amino Acids and Proteins Flashcards

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1
Q

How does epigenetic change gene expression?

A

methylation and histone modification

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2
Q

How is a peptide bond formed?

A

nucleophilic addition substitution between the C terminus of one AA and the N terminus of another

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3
Q

How are peptide bonds stabilized?

A

delocalization across the O and N on either side of the peptide bond

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4
Q

What is an AA in a polypeptide called?

A

residue

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5
Q

The N terminus is the?

A

amino group at the beginning

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6
Q

The C terminus is the?

A

carboxyl group at the end

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7
Q

What is pKa?

A

shows acid strength, lower the pKa the higher the acidity

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8
Q

Why is histidine useful to have an active sites?

A

Its side chain has a pKa of ~6.5 which is close to the physiological pH of ~7.4

Sensitive to pH change so it can stabilize or destabilize a substrate

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9
Q

pH < pKa

A

AA is protonated (+)

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10
Q

pH = pKa

A

mix of +/- AAs

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11
Q

pH > pKa

A

AA is deprotonated (-)

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12
Q

What’s weird about proline?

A

It has a 2* alpha amino group (side chain doubles back to bond with the N again)

This disrupts the alpha helix because the 2* alpha amino group causes kinks

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13
Q

What’s weird about glycine?

A

The simplest AA with side chain -H

Alpha carbon is no longer chiral (only nonchiral AA)

Disrupts the alpha helix because -H is so small which makes the molecule very flexible which causes kinks

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14
Q

What’s weird about cysteine?

A

Forms disulfide bridges if 2 get too close

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15
Q

CystEine vs cystine

A

Has the E if its reduced (SH)

No E if oxidized (S-)

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16
Q

Where are cysteine vs cystine?

A

extracellular = oxidizing = cystine

intracellular = reducing because of antioxidants = reduced = cystEine

17
Q

How to determine L vs D AA?

A

With COOH at the top and R at the bottom

If the amino group is on the Left = L

18
Q

Isoelectric point (pI)

A

the pH point where a molecule is net neutral

19
Q

How to find pI

A

take the average of pKas of all functional groups

20
Q

pH < pI

A

Everything is protonated = net +

21
Q

pH = pI

A

zwitterion = net neutral

22
Q

pH > pI

A

Everything is deprotonated = net -

23
Q

How are proteins 3* structure stabilized?

A

H bonding, Van der Waals forces, disulfide bridges, and hydrophobic packing

24
Q

solvation shell

A

the layer of solvent surrounding a protein which helps to stabilize (or destabilize) the outer layer