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Lecture 5

Protein folding & function

tertiary and quaternary structures are determined by primary structures; R-groups of AAs encoded by genome
T/F primary sequence has limited number of possible folding pathways TRUE
What are the forces stabilizing protein structure? TEST Hydrophobic effects H bonds Charge-charge interactions disulfide bonds metal ions (ex iron-heme group)
hetero vs homo dimer protein with multiple different polypeptide subunit=hetero homo has same polypeptide subunit
denaturation is protein unfolding, usually with loss of biological activity
why is there a loss of biological activity during denaturation because denaturation involves disruption of non-covalent bonds and thus loss of secondary and tertiary structures
how does are primary structures of proteins conserved during denaturation? denaturation is not strong enough to break the covalent peptide bonds, thus primary structure remains intact
types of denaturation? Heat– disturb weak bonds& 2ndary structures pH–change ionization state of R-groups, disrupting 2ndary structure (revert back to primary) chemicals–detergents (SDS)&chaotropic agents (urea) allow H2O to enter hydrophobic areas and disrupt normal folding
what do reducing agents do? break disulfide bonds (between cysteines) to get protein back to primary
what are some reducing agents? DTT β-mercaptoethanol
difference between protein reduction and denaturation? reduction breaks disulfide bonds denaturation breaks weak, noncovalent bonds
Anfinsen experiment? Ribonuclease treated with chaotrope (urea) and reducing agent ( β-mercaptoethanol)--> lost enzyme activity when denatured ribonuclease was dialyzed to remove urea and β-mercaptoethanol--> protein renatured, restoring activity
protein folding happens in__________ with several __________ endoplasmic reticulum intermediates
steps of protein structure unfolded secondary structure domains molten globule native tertiary structure
is protein folding always facilitated by proteins? in vivo, it is often facilitated by proteins can self assemble
what are chaperones binding proteins (loose association, not permanent) which assist in the formation of stable 3D protein structures in protein folding, most require ATP, different physical structures
what do chaperon protein do with misfolded/unfolded proteins - fix the misfiling (fold it correctly)+ take to destination - if cant help fix it, then take it to the "trash", degrades it
heat shock protein is an example of clamp type chaperon protein
GroEL-GroES protein complex is an example of chamber type chaperon protein
what do clamp type and chamber type proteins use to facilitate correct folding bind to misfolded protein and use ATP hydrolysis to fold
why is vitamin C important? because prolyl and lysl hydroxylase enzymes require Vitamin C as a coenzyme. Tendons can get "loose" as a result of scurvy
osteogenosis imperfecta glass bone disease cause brittle, pliable bones due to mutations in collagen genes α1 or α2 chains of type I collagen
Ehlers-Danlos Syndrome elastic skin/joints defect in collagen synthesis
how does a prion disease start misfolded version of the protein PrPsc, which acts as an infectious particle, interacts with PrPc (normal, wild type) version of the protein making it convert into mutant form
what are some prion diseases mad cow creutzefeldt-Jacob/kuru
what causes sickle cell? point mutation that changes glutamate to valine negatively charged AA to hydrophobic neutral causes cell to take on a sickle shape - ruptures easily, can aggregate and clump
Created by: rusulali97
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