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36 Cards in this Set

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diseases that resulted from protein folding gone wrong
mad cow, alzheimers, cystic fibrosis, emphysema, cancer
5 diseases
fundamental components of all living cells
misfolded proteins
poison the cells around it
what they do to the cells around them
christian anfinsen
if proteins become unfolded then they fold back into the propper shape, no shaper/folder needed
theory about when proteins unfold
keep proteins from getting off the right folding path
anfinsens theory to protein folding diseases
protiens will fold into a wrong shape

chaperones help fold
2 theories
1. protiens
2. chaperones
certain diseases are characterized by...
extensive protein deposits in certain tissues
what diseases are characterized by
alzheimer noted that...
neurofibrilary tangles and neuritic plaaque (dieseases that have extensive nerve cell death) are specific to alzheimers
neurofibrilary tangles
neuritic plaque
key to a-helix and b-sheet
hydrogen bond
type of bond
number of amino acids for each turn of the a-helix
3.6 amino acids
decimal number
right hand spiral stabilized by hydrogen bonds btwn each amino acid (nitrogen atom and the oxygen atom) of the fourth one up the chain
what type of spiral
what type of bonds
number up the chain


flat with sides of the chain sticking out on alteranate sides, stabilized by hydrogen bonds btwn nitrogen and oxygen atoms, amino acid chains run alongside each other

parallel- run in same direction

antiparallel- alternate chains run in opposite directions
flat or round?
what sticks out
what type of bonds
antiparallel sheets

often formed by one chain looping back on itself
b-turn- the 1 to 3 amino acids linking 2 strands
what does it do
partially folded chains
fold in a fraction of a second
how long
virus that infects bacteria
virus or bacteria?
high temp. sensitive mutations
one amino acid altered and turns into insoluble gunk, able to analyze bacterial cells to see what went wrong with the folding
whats altered
what happens at high temps
scientists analyze what
peripheral nerves and other organs are damaged by deposists of amyloid-type protein, rare disease, transthyretin mutations (b-sheets, identical amino acid chains) 50 different mutations
whats damaged by amyloid-type protein
rare or not rare disease?
what type of mutations
how many
transthyretin aggregation
monomeric unfolding intermediate
monomeric what
normal transthyretin, when protein is broken down it turns to insoluble gunk that poisons the tissues where it is deposited
normal what?
when protein breaks down what happens?
alzheimers afflicts...
10% of those over 65
50% of those over 85
kills 10,000 each year
costs $82.7 billion
amyloid precursor protein mutations develop alzheimers as early as 40
what % over 65
what % over 85
kills how many each year
costs how much each year
neuritic plaque
pathway leading to alzheimers
pathway leading to what
alzheimers disease is limited...
to old people b/c the process takes a long time, have the normal amyloid precursor protein
what type of ppl and why
have normal what protein
trasports cholesterol and other fatty materials in the blood stream, rapid formation of plaque
transports what
rapid formation of what
AB plays a major roll in __ disease
what disease
protein particles, pure protien that contain neither DNA or RNA, self replicating (own chaperone)
what type of particles
doestn contain what and what
what does it do (replicate)
mad cow (scrapie, creutzfeldt-jacob)
diseases transmitted by prions
transmitted by what
cystic fibrosis
lack of protein that regulates the transport of the chloride ion across the cell membrane
lack of what
regulates what across what
cystic fibrosis hinders...
seperation of the transport regulator protein from one of its chaperones, final steps in folding cant occur, normal amounts of active protein arent produced
seperation of what from what
final steps in what cant occur
normal amounts of what arent produced
buildup of a crucial folding intermediate leads to aggregation which deprives some of enough circulating a1 antitrypsin to protect lungs
buildup of what
leads to what that deprives some of what al antitryspin to do what to the lungs
purpose of studying diseases
find ways to treat it
find ways to do what
involved in 40% of all human cancers, prevents cells from becoming cancerous
what % of all cancers
prevents what
p53 (2 clases)
1.keeps protein from binding to DNA
2.makes folded form of protein less stable
1.keeps what from happening
2.makes what less stable
TIP and the thyroid hormone
can stabilize transthyretin and is a treatment for FAP
once folding is complete...
chaperone will leave its protein to help another
what a chaperone does once folings done
how many chaperones can there be
one or several?
chaperones primary function
prevent aggregation
to prevent what