Intro to Biochem- Study Materials for
Exam 1- Murphy Questions and
Answers 100% Pass
why are non-covalent bonds important - ✔✔10-100x weaker than covalent, energies are
cumulative, include electrostatic, dispersion, H bonds
What else are non-covalent bonds involved in - ✔✔define structure and function, binds
hGH, amino acids involved in ligand/receptor bindings
charge charge E distance - ✔✔1/r
charge dipole - ✔✔1/r^2
dipole dipole - ✔✔1/r^3
charge induced dipole - ✔✔was neutral but when charge came up created dipole 1/r^4
dipole induced dipole - ✔✔1/r^5
dispersion (van der waals) - ✔✔1/r^6
H bond donor - ✔✔with H
Katelyn Whitman, All Rights Reserved © 2025 1
,H bond acceptor - ✔✔no H
dielectric constant - ✔✔relative permitivity when medium is between charges screening
them from one another, waters is high
H bonding - ✔✔electron sharing is highly directional, charge/charge interaction, high
energy bonds, short fixed bond length
boiling point - ✔✔increases with molecular mass except when H bonding happens
(high BP)
adhesion - ✔✔attraction between different molecules
cohesion - ✔✔attraction between same molecules
surface tension - ✔✔how easy/difficult it is to break/stretch surface
water's unique properties - ✔✔2 H bond donor sites, 2 H bond acceptor sites,
permanent dipole, high heat capacity, density greater in liquid, relatively high dielectric
constant
hydrophilic molecules in water - ✔✔solvent can compete with intramolecular H bonds,
sometimes stabilizing, sometimes destabilizing, ions get hydration shells
hydrophobic molecules in aqueous solution - ✔✔clathrate structures hide nonpolar
molecules (energetically favorable)
Katelyn Whitman, All Rights Reserved © 2025 2
, hydrophobic effect - ✔✔stabilizes protein structure by driving apolar side chains on
amino acids together to minimize formation of this ordered structure
amphipathic molecules in aqueous solution - ✔✔monolayer, micelle, or bilayer
Henderson Hasselbach - ✔✔pH = pKa + log([A-]/[HA])
Ka - ✔✔dissociation constant
when are buffers excellent - ✔✔pH is pKa, group is 50% protonated
deprotonated means - ✔✔ionized
pH < pKa - ✔✔HA > A-
pH = pKa - ✔✔HA= A-
pH > pKa - ✔✔HA < A-
isoelectric point - ✔✔no charge, average of pKa's of +1 and -1 species
ionic properties of amino acid side chains - ✔✔impart ionic properties to proteins like
pH
isoelectric focusing - ✔✔moves in gel based on pH
protein - ✔✔amino acid, peptide bond
polysaccharide - ✔✔monosaccharide, glycoside
Katelyn Whitman, All Rights Reserved © 2025 3
Exam 1- Murphy Questions and
Answers 100% Pass
why are non-covalent bonds important - ✔✔10-100x weaker than covalent, energies are
cumulative, include electrostatic, dispersion, H bonds
What else are non-covalent bonds involved in - ✔✔define structure and function, binds
hGH, amino acids involved in ligand/receptor bindings
charge charge E distance - ✔✔1/r
charge dipole - ✔✔1/r^2
dipole dipole - ✔✔1/r^3
charge induced dipole - ✔✔was neutral but when charge came up created dipole 1/r^4
dipole induced dipole - ✔✔1/r^5
dispersion (van der waals) - ✔✔1/r^6
H bond donor - ✔✔with H
Katelyn Whitman, All Rights Reserved © 2025 1
,H bond acceptor - ✔✔no H
dielectric constant - ✔✔relative permitivity when medium is between charges screening
them from one another, waters is high
H bonding - ✔✔electron sharing is highly directional, charge/charge interaction, high
energy bonds, short fixed bond length
boiling point - ✔✔increases with molecular mass except when H bonding happens
(high BP)
adhesion - ✔✔attraction between different molecules
cohesion - ✔✔attraction between same molecules
surface tension - ✔✔how easy/difficult it is to break/stretch surface
water's unique properties - ✔✔2 H bond donor sites, 2 H bond acceptor sites,
permanent dipole, high heat capacity, density greater in liquid, relatively high dielectric
constant
hydrophilic molecules in water - ✔✔solvent can compete with intramolecular H bonds,
sometimes stabilizing, sometimes destabilizing, ions get hydration shells
hydrophobic molecules in aqueous solution - ✔✔clathrate structures hide nonpolar
molecules (energetically favorable)
Katelyn Whitman, All Rights Reserved © 2025 2
, hydrophobic effect - ✔✔stabilizes protein structure by driving apolar side chains on
amino acids together to minimize formation of this ordered structure
amphipathic molecules in aqueous solution - ✔✔monolayer, micelle, or bilayer
Henderson Hasselbach - ✔✔pH = pKa + log([A-]/[HA])
Ka - ✔✔dissociation constant
when are buffers excellent - ✔✔pH is pKa, group is 50% protonated
deprotonated means - ✔✔ionized
pH < pKa - ✔✔HA > A-
pH = pKa - ✔✔HA= A-
pH > pKa - ✔✔HA < A-
isoelectric point - ✔✔no charge, average of pKa's of +1 and -1 species
ionic properties of amino acid side chains - ✔✔impart ionic properties to proteins like
pH
isoelectric focusing - ✔✔moves in gel based on pH
protein - ✔✔amino acid, peptide bond
polysaccharide - ✔✔monosaccharide, glycoside
Katelyn Whitman, All Rights Reserved © 2025 3
