BIOSC 0150 Study Guide - Quiz Guide: Disulfide, Exergonic Reaction, Ionic Bonding
5 Apr 2018
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Document Summary
At neutral ph, zwitter ions exist both ionized, nh3+ and coo- so each is charged, but overall is neutral, then a charge can be added with r groups. Adding atp for e consists of removing the phosphate group from atp and adding it. When release phosphate group from the atp, it releases a lot of energy, and adding that phosphate group to another molecule is endergonic but doesnt take as much energy as the first part releass. Tertiary: hydrogen bonds, hydrophobic interactions, van der waals, disulphide bonds, ionic bonding between side chains with opposite charges (only acidic and basic r groups) Quaternary structure: hydrogen bonds, disulfide bridges, salt bridges. Salinity: if put in an envt with a bunch of salts in it, affects the salt bridges. Cofactors are parts of an enzyme that help it function, cofactors are always there, not dependent on substrate being there. Induced fit: the act of the substrate bonding to the enzyme changes its shape.
