FIRST PUBLISH OCTOBER 2024
Intro to Biochem- Study Materials for
Exam 1- Murphy Study Guide
why are non-covalent bonds important - Ans:✔✔-10-100x weaker than covalent, energies are
cumulative, include electrostatic, dispersion, H bonds
What else are non-covalent bonds involved in - Ans:✔✔-define structure and function, binds hGH, amino
acids involved in ligand/receptor bindings
charge charge E distance - Ans:✔✔-1/r
charge dipole - Ans:✔✔-1/r^2
dipole dipole - Ans:✔✔-1/r^3
charge induced dipole - Ans:✔✔-was neutral but when charge came up created dipole 1/r^4
dipole induced dipole - Ans:✔✔-1/r^5
dispersion (van der waals) - Ans:✔✔-1/r^6
H bond donor - Ans:✔✔-with H
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H bond acceptor - Ans:✔✔-no H
dielectric constant - Ans:✔✔-relative permitivity when medium is between charges screening them from
one another, waters is high
H bonding - Ans:✔✔-electron sharing is highly directional, charge/charge interaction, high energy bonds,
short fixed bond length
boiling point - Ans:✔✔-increases with molecular mass except when H bonding happens (high BP)
adhesion - Ans:✔✔-attraction between different molecules
cohesion - Ans:✔✔-attraction between same molecules
surface tension - Ans:✔✔-how easy/difficult it is to break/stretch surface
water's unique properties - Ans:✔✔-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 - Ans:✔✔-solvent can compete with intramolecular H bonds, sometimes
stabilizing, sometimes destabilizing, ions get hydration shells
hydrophobic molecules in aqueous solution - Ans:✔✔-clathrate structures hide nonpolar molecules
(energetically favorable)
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FIRST PUBLISH OCTOBER 2024
hydrophobic effect - Ans:✔✔-stabilizes protein structure by driving apolar side chains on amino acids
together to minimize formation of this ordered structure
amphipathic molecules in aqueous solution - Ans:✔✔-monolayer, micelle, or bilayer
Henderson Hasselbach - Ans:✔✔-pH = pKa + log([A-]/[HA])
Ka - Ans:✔✔-dissociation constant
when are buffers excellent - Ans:✔✔-pH is pKa, group is 50% protonated
deprotonated means - Ans:✔✔-ionized
pH < pKa - Ans:✔✔-HA > A-
pH = pKa - Ans:✔✔-HA= A-
pH > pKa - Ans:✔✔-HA < A-
isoelectric point - Ans:✔✔-no charge, average of pKa's of +1 and -1 species
ionic properties of amino acid side chains - Ans:✔✔-impart ionic properties to proteins like pH
isoelectric focusing - Ans:✔✔-moves in gel based on pH
protein - Ans:✔✔-amino acid, peptide bond
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