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Write methyl

Ethyl

Phenyl

Carbonyl (aldehyde)

Carbonyl (ketone)

Carboxyl

Hydroxyl (alcohol)

Enol

Ether

Ester

Acetyl

Anhydride

Amino

Amido

Imine

N-Subsituted Imine
Schiff Base

Guanidinium

Imidazole

Sulfhydryl

Disulfide

Thioester

Phosphoryl

Phosphoanhydride

Mixed anhydride
carboxylic acid and phosphoric acid: acyl phosphate

What are the prefixes for nano, micro, and mili?
nano: 10 -9
micro: 10 -6
mili: 10 -3
How do you know what the stronger acid is based off the Keq?
the larger the Keq is, the stronger the acid
How does pKa determine how strong an acid is?
lower pKA= stronger acid
At what pH does concentration of acid equal that of its conjucate base?
when pH=pKa
Define what a buffer is and explain how a buffer system works.
maintains constancy of pH with weak acid and conjucate base
flattest point on titration curve
At what pH does a cmpd have maximium buffering capacity?
When pH= pKa
What is the pH range over which the cmpd is useful as a buffer?
the flat portion
Glycine
Gly, G

Alanine
Ala, A

Proline
Pro, P

Valine
Val, V

Leucine
Leu, L

Isoleucine
Ile, I

Methionine
Met, M

Phenylalanine
Phe, F

Tyrosine
Tyr, Y

Tryptophan
Trp, W

What has a lower pKa value?
carboxylic acid --> this means the H gets deprotonated off of here first
What is the first rule of thumb to see if something has a polar side chain?
If it has N, O, or S
How can you tell when something will be a hydrogen bond acceptor vs donor?
acceptor: any molecule that has a relatively electronegative atom
donor: electronegative atom bond to a hydrogen
If the pH is below the pKA, what form is it in?
protonated so its pos
What are the exceptions to the polar side chain rule, these are actually?
Tyr, Trp, Cys, Met
- nonpolar
What is the hydropathy index?
tells you if it is hydrophobic or hydrophilic
pos: hydrophobic
neg: hydrophilic
Which amino acids can hydrogen bond?
ASK
Which amino acids can interact ionically?
lysine, arginine, histidine, aspartate, glutamate, tyrosine, cysteine
What is the general rule of thumb when looking at how pH is relative to pKa?
2 units below pKa: 0.01
1 unit below: 0.1
= pKa: 1
1 unit above: 10.0
2 units above: 100
What are most amino acids?
zwitterions: neutral amino acid
How should you solve which 2 forms of an amino acid predominate at any given pH value?
draw out titration curve: make the first one fully protonated
and then go from there
How do you determine the PI of the amino acid that has ionizable side chains?
take the average of the pKA of the ones that are flanking the neutral amino acid
What is the structure of the peptide bond, draw out the full one with N terminal and C terminal

Serine
Ser, S

Threonine
Thr, T

Cysteine
Cys, C

Asparagine
Asn, N

Glutamine
Gln, Q

What should you look at when seeing how many hydrogen bonds a molecule can form?
O and N with lone pairs --> 2 lone pairs, 2 hydrogen bonds
Then look for number of hydrogens that can accept
What happens to entropy when you place a hydrophobic molecule in water? How can we minimize this?
When you place a hydrophobic molecule in water, the entropy of water decreases
We can minimize this by allowing the hydrophobic molecules to aggregate--> this is called the hydrophobic effect
How do you know when an amino acid is drawn in the L configuration?
amino group is on the left, all amino acids in proteins are in L configiguration
What is important when seeing the word predominate?
It needs to be above or below that pKa value, at the pKa value it is equal
How do you know the dirction of migration?
When a pH is below the pI, it is protonated so it is pos so it will move to the negative side
What is an ester made up of?
carboxylic acid and alcohol
What is an amide made up of?
acid and ammonia
What is an acid anhydride made up of?
2 molecules of acetic
What are the 4 types of non-covalent interactions that stabilize biomolecules?
hydrogen, ionic, van der Waals, hydrophobic effect
Negatively charged R groups are?
acidic
Lysine
Lys, K

Arginine
Arg, R

Histidine
His, H

Aspartate
Asp, D

Glutamate
Glu, E

What is a phosphoester?
R-CH2 and then phosphate group with another R
How do you calculate the charge on a peptide?
use the pH, find the forms that are deprotonated/protonated--> then add up the overall charge