w3 biol200

give an example of a missense mutation

dark-coated mainland mice colonize a beach habitat. At some point, a point mutation occurred in the population that altered the melanocortin receptor gene and resulted in offspring with light coats

missense mutation definition

a type of point mutation where single base change in DNA sequence results in a different amino acid in the resulting protein

silent mutation

Does not result in any amino acid change in protein, it is when a mutation occurs in DNA but the resulting codon still corresponds to the same amino acid

nonsense mutation

type of point mutation that changes a codon corresponding to a different amino acid is changed into a stop codon, causing premature termination

effect of nonsense mutation

almost always destroys function of the protein

effects a mutation can have on an organism’s fitness

Beneficial, neutral, deleterious

most point mutations are

slightly deleterious or neutral

base sequence of start codon corresponding amino acid

AUG, methionene

Start codon initiates translation and codes for an amino acid, stop codons signal end of translation and

do not code for amino acid

amino acids linked by peptide bonds are referred to as

residues

peptide bonds are

bonds between amino acids

The release factor’s role is to

catalyze the hydrolysis of the bond between the last tRNA and the

completed protein.

How do enzymes increase the rate of reaction (don’t just say they lower activation energy)

they lower activation energy by stabilizing the molecule in the transition state, thus lowering the energy required to get the reaction to the transition state. This does not impact the net change of energy released/absorbed (gibbs)

how fast will hydrophobic molecule cross cell membrane

very quickly, dissolve easily in lipid core of bilayer

how easily can charged molecules (ions) pass through bilayer?

not as easily, the charge of ions attracts water molecules and it requires a lot of energy to remove them so that the ion can diffuse without any sort of protein channel

what is tertiary structure interaction

all chemical interactions: h-bonding, hydrophobic (van der waal) , hydrophilic, ionic bonds, disulfing bonds