slide 19 - protein folding and structure

hydrophobic-hydrophillic

can affect protein folding

negative-postiive

can repel what it used to be attracted to

small-bulky

can hinder protein folding and functions

protein activity is controlled by

post-translational modifications

phosphorylation

add phosphate group

ubiquination

small protein usually added to mark it for degradation

ubiquination allows for

repid turnover of regulatory proteins for cell function, quality control to identify and destroy misfolded or damaged proteins

UPS

ubiquinatin proteasome system

UPS purpose

degrades poly-ubiquitylated proteins

UPS steps

E1, E2, E3, 4

E1 ubiquitin-activating enzyme

uses ATP to activate ubiquitin

E2 ubiquitin conjugating enzyme

recived ubiquitin from E1 and binds to E3

E3 ubiquitin ligase

recognizes specific protein target transfers ubiquitin from E2 to target protein

step 4

proteins with multiple ubiquitin proteins attached are chewed up by proteasome

silent mutation

nucleotide charge does not change amino acid coding

missense mutation

nucleotide change resulting in an amino acid change, impact on protein structure and function

frameshift mutation

insertion or deletion that shifts teh reading fram = bad

nonsense mutaiton

mutation that results in a premature usually bad affect on protein folding