Protein Structure Flashcards
What is the -log of 0.0001?
Scientific would be 1 x 10^ -4 so log would be -4 therefore:
-log = 4
PKa of strong acids? Why?
Formula for pKa?
Strong acids do not have a pKa because they completely dissociate
PKa= -log (Ka)
The ___ the pKa, the stronger the weak acid
Lower
(So a slight amount of dissociation = larger pKa
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?
PH= pKa + log ([conj. Base]/[acid])
Equation become pH = pKa because the log of 1 = 0
Buffering and drug absorption
The log of a number less than one is?
So if [conjugate base] < [acid], then?
Negative
PH would be lower than the pKa
- What happens if you add an acid to a buffered solution?
2. What happens if you add a base to a buffered solution?
- Excess protons will bind to the conjugate base
2. The weak acid will dissociate H+ to neutralize the excess base
- What is the most effective buffering range?
2. A more concentrated buffer in solution contains ___ buffer molecules to react with acid or base
- +/- 1 pH untif of the pKa of the weak acid
2. More (buffer capacity increases with concentration)
- When pH of solution > pKa, [__] > [___]
2. When pH of solution < pKa, [__] < [__]
- [conj base] > [acid]
2. [conj base] < [acid]
- If pH > pKa, the system has acquired ___ and more ___ will be formed
- If pH < pKa, the system has acquired more __ and more __ will be formed
- Acquired OH- ions, and more conjugate base will be formed
2. H+, more acid
COO is going to protonated at what pHs?
NH is going to be protonated at what pHs?
R-COOH at pH less than 7 (increases H+ concentration)
R-NH3+ at pH less than 7 (increases H+ concentration)
What ion causes pH to rise
Bicarbonate ion (HCO3-)
PKa of NH2 is 6.0-11.0. When would it be deprotonated?
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)
Does the charged or uncharged form get absorbed?
Uncharged (so not COO- or NH3+)
What is primary structure?
Sequence of amino acids
- Two secondary structures?
- Proline affects which of these structures?
- Difference between the structure of alpha helices and beta sheets
- Alpha helix and beta sheet
- Alpha helix (can cause kinks)
- Both have hydrogen bonds but alpha helices are tightly coiled and beta sheets are stretched out
- What is tertiary structure
2. 4 main interactions involved in this process?
- Final 3D form of a SINGLE polypeptide
- Disulfide bonds, hydrophobic interactions, hydrogen bonds(partial charge interaction between R groups), and ionic bonds
___ R-group interactions contribute significantly to stability of tertiary structure
Nonpolar
Ionic bonds are formed between?
R groups of positively and negatively charged amino acids (or other fully charged molecules)
Main distinctions between hydrogen bonds and ionic bonds?
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
- What is quaternary structure?
- Only present in proteins that ?
- Example?
- Structural interactions between individual polypeptide chains to form the protein
- Have more than one polypeptide chain
- Hemoglobin (has 4 polypeptides: 2 alpha chains and 2 beta chains)