Studied by 6 peopleAsparate
(asp). Acidic side group
Glutamate
(glu). Acidic side group
Arginine
(arg). Basic side group
Lysine
(lys). Basic side group
Cysteine
(cys). Sulfur containing.
Proline
(pro). Kink-inducing
Cysteine folding
Two adjacent cysteins form a disulfide bond. In the cytoplasm they remain reduced but they readily form in oxidizing environments.
Ionic bonding
The acidic and basic amino acids form these.
isoelectric point
the pH at which a protein is no longer donating or accepting protons, it is neutral.
Secondary protein structure
local folding driven by hydrogen bonds. alpha and beta helices
alpha helices
all side chains outward, vertical hydrogen bonding. Within one peptide chain.
beta helices
side chains alternate pointing up and down. These are across two peptide chains
Reading amino acid chains
Read N to C. Amine to carbon with R group to carbonyl.
Sickle cell anemia
At position 6, Glu becomes Val. Val is extremely hydrophobic and so hemoglobin tries to bury it but new Val become exposed and so stacking occurs and this causes the blood cells to sickle. This makes it harder for red blood cells to move through arteries and causes finger swelling.
Hydrophobic interactions
decrease mobility of water along hydrophobic surfaces causes a decrease in entropy which disrupts hydrogen bonding and hydrophobic residues cluster.
Amino acids
Composed of an amine, a carboxylic acid, and an R group. pH of ~ 7.4
Note
Flashcard