Protein Structure Flashcards

1
Q

What is the -log of 0.0001?

A

Scientific would be 1 x 10^ -4 so log would be -4 therefore:

-log = 4

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2
Q

PKa of strong acids? Why?

Formula for pKa?

A

Strong acids do not have a pKa because they completely dissociate

PKa= -log (Ka)

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3
Q

The ___ the pKa, the stronger the weak acid

A

Lower

(So a slight amount of dissociation = larger pKa

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4
Q

What is the henderson hasselbach equation?

What does this equation become when conjugate base concentration = acid concentration?

2 things this equation is used to predict?

A

PH= pKa + log ([conj. Base]/[acid])

Equation become pH = pKa because the log of 1 = 0

Buffering and drug absorption

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5
Q

The log of a number less than one is?

So if [conjugate base] < [acid], then?

A

Negative

PH would be lower than the pKa

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6
Q
  1. What happens if you add an acid to a buffered solution?

2. What happens if you add a base to a buffered solution?

A
  1. Excess protons will bind to the conjugate base

2. The weak acid will dissociate H+ to neutralize the excess base

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7
Q
  1. What is the most effective buffering range?

2. A more concentrated buffer in solution contains ___ buffer molecules to react with acid or base

A
  1. +/- 1 pH untif of the pKa of the weak acid

2. More (buffer capacity increases with concentration)

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8
Q
  1. When pH of solution > pKa, [__] > [___]

2. When pH of solution < pKa, [__] < [__]

A
  1. [conj base] > [acid]

2. [conj base] < [acid]

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9
Q
  1. If pH > pKa, the system has acquired ___ and more ___ will be formed
  2. If pH < pKa, the system has acquired more __ and more __ will be formed
A
  1. Acquired OH- ions, and more conjugate base will be formed

2. H+, more acid

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10
Q

COO is going to protonated at what pHs?

NH is going to be protonated at what pHs?

A

R-COOH at pH less than 7 (increases H+ concentration)

R-NH3+ at pH less than 7 (increases H+ concentration)

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11
Q

What ion causes pH to rise

A

Bicarbonate ion (HCO3-)

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12
Q

PKa of NH2 is 6.0-11.0. When would it be deprotonated?

A

NH2 wants to be protonated (NH3+) so it will be protonated unless pH > 11 (because at that point there would be no other hydrogens around so NH3+ would have to give it up)

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13
Q

Does the charged or uncharged form get absorbed?

A

Uncharged (so not COO- or NH3+)

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14
Q

What is primary structure?

A

Sequence of amino acids

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15
Q
  1. Two secondary structures?
  2. Proline affects which of these structures?
  3. Difference between the structure of alpha helices and beta sheets
A
  1. Alpha helix and beta sheet
  2. Alpha helix (can cause kinks)
  3. Both have hydrogen bonds but alpha helices are tightly coiled and beta sheets are stretched out
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16
Q
  1. What is tertiary structure

2. 4 main interactions involved in this process?

A
  1. Final 3D form of a SINGLE polypeptide
  2. Disulfide bonds, hydrophobic interactions, hydrogen bonds(partial charge interaction between R groups), and ionic bonds
17
Q

___ R-group interactions contribute significantly to stability of tertiary structure

18
Q

Ionic bonds are formed between?

A

R groups of positively and negatively charged amino acids (or other fully charged molecules)

19
Q

Main distinctions between hydrogen bonds and ionic bonds?

A

Ionic bonds - both components are fully ionized and have opposite charges

Hydrogen bonds- hydrogen only has a partial positive charge that interacts with other negative charges / negative partial charges

20
Q
  1. What is quaternary structure?
  2. Only present in proteins that ?
  3. Example?
A
  1. Structural interactions between individual polypeptide chains to form the protein
  2. Have more than one polypeptide chain
  3. Hemoglobin (has 4 polypeptides: 2 alpha chains and 2 beta chains)