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