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protein synthesis occurs in
the cytosol
rate limiting step of translation
first amino acid being placed
redundancy/degeneracy
usually manifests in 3rd nucleotide (wobble position)
Hsp70
chaperone proteins that bind to the polypeptide and protect against misfolding, can be facultative or constitutive
Hsp60
forms a cylindrical barrel to achieve proper folding and 3d conformation of the protein
polysome
one mRNa has many ribosomes attached, each making their own protein
signaling sequence in polypeptide
will pause translation and move the protein ribosome complex to the cisternae of the ER
rough ER
synthesizes ribosomes
smooth er
abundant in ovaries, liver, and testes
makes lipids
functions in detox reactions
steps of traslation involving ER
protein begins synthesis on the free ribosome
signal sequence on N terminus is reached
SRP binds to signal sequence
attahces to the ER lumen
translation continues
signal peptidase cleaves polypeptide
polypeptide may be packaged into vesicles and secreted
binding proteins
chaperone proteins that may attach to the polypeptide inside the lumen of the ER to prevent misfolding
vesicles leaving ER
vesicles move proteins between cisternae
moves to cis face of golgi
delievered out of trans face to fuse with PM
stop codons in ER
allow transmembrane proteins to form, termini can go either way
modifications that occur in the lumen of the ER
N glycosylation
disulfide bonds
GPI lipid link
N glycosylation
addition of sugar to the N of asparagine
protective against proteases
functions in recognition in the ECF
GPI linkages
protein has signal and stop sequences for TM protein
start transfer peptide cleaved off
protein is cleave and transferred to GPI lipid anchor
Hematouria
red blood cells get destroyed by immune system cells that mistakenly target their lack of lipid link
disulfide bond formation
occurs in oxidative ER lumen
get broken and reformed by protein disulfide isomerase