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Intro to Biochem- Study Materials for Exam 1- Murphy Exam 2024/2025 Questions With Completed & Verified Solutions. $9.99   Add to cart

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Intro to Biochem- Study Materials for Exam 1- Murphy Exam 2024/2025 Questions With Completed & Verified Solutions.

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  • Rutgers Murphy Biochem Exm 2
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  • Rutgers Murphy Biochem Exm 2

Intro to Biochem- Study Materials for Exam 1- Murphy Exam 2024/2025 Questions With Completed & Verified Solutions.

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  • August 23, 2024
  • 13
  • 2024/2025
  • Exam (elaborations)
  • Questions & answers
  • charge dipole ans 1r2
  • Rutgers Murphy Biochem Exm 2
  • Rutgers Murphy Biochem Exm 2
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phylliswambui
Intro to Biochem- Study Materials for
Exam 1- Murphy

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

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)

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

polysaccharide - ANS monosaccharide, glycoside

nucleic acid - ANS nucleotide, phosphodiester

lipids - ANS fatty acids, ester

biopolymers - ANS nucleic acid, carbohydrates, proteins

characteristics of living matter - ANS program, improvisation, compartmentalization, energy,
regeneration, adaptability, seclusion

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