Chapter 1 review Flashcards
All chiral amino acids are S/R
All chiral amino acids are S
Cysteine is chiral (T/F)
T
_____ is chiral but is R configuration
Cysteine
What is an amino acid that is not chiral
Glycine
R group of glycine
H
Nonpolar, nonaromatic amino acids
GAVL IMP
Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Proline
Aromatic amino acids
Tryptophan, phenylalanine, tyrosine
Polar amino acids
SAT GC
Serine, Asparagine, Threonine, Glutamine, Cysteine
Negatively charged amino acids
Aspartate, glutamate
Positively charged amino acids
Lysine, Arginine, Histidine
Term used to describe having both the ability to donate or receive protons
Amphoteric
pKa definition
pH at which half of the species are deprotonated
At pH near pI, amino acids are in their _____ form
Zwitterion
Formula to calculate pI for uncharged amino acid
Averaging two pKa values
Briefly describe the titration curve for an amino acid
Nearly flat at pKa values of amino acid. Nearly vertical at pI of amino acid
Amino acid with charged side chain has additional pKa value. How is this calculated?
Average of pKa value at which zwitterion is protonated and deprotonated
pI of amino acid without charged side chain
6
Acidic amino acid pI
Below 6
Basic amino acid pI
Above 6
What is the amino acid responsible for interrupting the secondary structure?
Proline
Name the interaction responsible for pushing hydrophobic R groups to the interior of the protein
Hydrophobic interaction
Describe what a disulfide bond is
Two cystine molecules are oxidized and create a covalent bond to form cysteine
Name of proteins with covalently attached molecules
Conjugated proteins
Name of group covalently attached to conjugated proteins. Give examples.
Prosthetic groups. Metal ions, vitamins, lipid, carbs, nucleic acid
Two ways denaturation can happen
- Heat
- Solvent (solute concentration)