1 Flashcards
(25 cards)
what bonds link AA in proteins
peptide/amide. they are covalent
what bonds link monosaccharides
glycosidic
what bonds link nucleotides
phosphodiester
can a protein be in multiple categories (enzyme/transporter/lipoprotein)
yes
biochemistry is study of
chemical processes within living organisms
what causes sickle cell
single amino acid change in hemoglobin
what is a h bond donor
hydrogen on electronegative atom
h bond acceptor
lone pairs on electroneg atom
how does psilocin work
it binds to serotonin receptors. psilocybin also does, just less
how are cofactors bound
covalently or noncovalently
transporters bind molecules they transport using what type of bond
noncovalently
protein cofactor
non protein molecule (no AA) and metal ions that assist with structure and/or function
proethetic group
subset of cofactor. group of larger chemicals bound covalently.
coenzyme
type of cofactor that shuttles commonly used functional groups in chemical reactions. like a phosphate donor to another enzyme
metal ion cofactors do what
bind to functional groups of opposite charge to help with structure or enzyme catalysis. for example it can change protein structure to create cavities so the protein can bind to other things
backbone cartoon or ribbon diagram contains
just peptide bonds
surface filling model contains what
all atoms, with amino acid side chains
red is for what atom in 3d structures
oxygen
blue is for what atom in 3d structures
nitrogen
how many transient h bonds can water form
4, due to unequal sharing of electrons (two electron pairs and 2 hydrogens)
main driving force for macromolecular structure
hydrophobic effect (nonpolar molecules aggregate, excluding water molecules) and hydrogen bonds
what does aggregation of nonpolar molecules in water do to entropy
increase in total entropy, because water entropy increased a crap ton, and nonpolar molecule entropy decreased a little
water can participate in what because it is a great nucleophile
hydrolysis and condensation (releasing water)
why do you need to consider binding interactions and intermolecular forces for drug design
presence or absense of functional groups can assist with solubility and binding