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Intro to Biochem- Study Materials for Exam 1- Murphy Study Guide
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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...

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  • October 23, 2024
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©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED

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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, ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED

FIRST PUBLISH OCTOBER 2024




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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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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