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chemistry notes
Term | Definition |
---|---|
lysine | found in proteins |
adenine | component of nucleic acids |
epinephrine | neurotransmitter in brain; hormone released during stress |
constitutional isomers | same number of atoms of each element ex-butane,pentane,2-methylpropane |
optical isomers | pair of isomers that are mirror images of each other ex-3-methylhexane, alanine |
geometric isomers | each of two or more compounds which differ from each other by arrangement to double bond, rings ex-trans-2-butene |
addition reaction | r-ch = ch-r + x-y --> r-ch^x - ch^y - r |
elimination reaction | r-ch^x-ch^y-r --> r-ch=ch-r +x-y |
substitution reaction | r-c-x + : y ---> r-c-y + : x |
rearrangement reaction | ch3 - ch2 - ch2 - ch3 ---> ch3 - ch ^ch3 (under ch3) |
decomposition/elimination | piece of the molecule breaks off as in formation of free radicals in polymerization reactions |
INTRAmolecular forces (bonding) | the forces that hold the atoms in a molecule together |
INTERmolecular forces (non-bonding) | the forces between two molecules |
ion-dipole forces | exist between an ion and the partial charge on an atom in a polar molecule |
dipole-dipole forces | exist between the partial charges on atoms in two polar molecules |
hydrogen bonding | only between atoms of very high electronegativity (ex-N,O,F,S and H2O) |
london dispersion | always present for all solutions |
non-polar side chains include? | - alanine - glycine - isoleucine - leucine - methionine - phenylalanine - proline - tryptophan - valine |
polar side chains include? | - asparagine - glutamine - tyrosine - cysteine - serine - threonine |
basic side chains include? | - aspartic acid - glutamic acid |
acidic side chains include? | - arginine - histidine - lysine |
a- amino group is? | primary |
proline is? | secondary |
if a strong acid is added the zwitterion is? | a positive ion |
if a strong base is added the zwitterion is? | a negative ion |
what is the isoelectric point? | the pH at which the molecules of a compound in solution have no net charge, (natural overall) |
primary structure | sequence of amino acids in a polypeptide chain (from N to C) |
secondary structure | conformations of amino acids in localized regions of a polypeptide chain (a-helix, b-pleated sheet, random coil) |
tertiary structure | the complete 30 arrangement of atoms of a polypeptide chain |
quaternary structure | the spatial relationship+interactions between subunits in a protein that has more than one polypeptide chain |
a-helix | 3.6 amino acids per turn of the helix |
b-pleated sheet | the c=o and n-h groups of the peptide bonds from adjacent chains point towards each other |
denaturation | the process of destroying the conformation of a protein by chemical/physical means |
enzymes | provide an alternative pathway for reaction; are all proteins |
oxidoreductases | oxidation-reduction reactions |
transferases | group transfer reactions |
hydrolyses | hydrolysis reactions |
lyases | addition of two groups to a c-c double bond |
isomerases | isomerization reactions |
ligases | the joining of two molecules |
mimicry | transition state analog = molecule whose shape mimics the transition of a substrate |