Protein Folding

Front 1

diseases that resulted from protein folding gone wrong

Back 1

mad cow, alzheimers, cystic fibrosis, emphysema, cancer

Hint 1

5 diseases

Front 2

proteins

Back 2

fundamental components of all living cells

Hint 2

definition

Front 3

misfolded proteins

Back 3

poison the cells around it

Hint 3

what they do to the cells around them

Front 4

christian anfinsen

Back 4

if proteins become unfolded then they fold back into the propper shape, no shaper/folder needed

Hint 4

theory about when proteins unfold

Front 5

chaperones

Back 5

keep proteins from getting off the right folding path

Hint 5

definition

Front 6

anfinsens theory to protein folding diseases

Back 6

protiens will fold into a wrong shape

chaperones help fold

Hint 6

2 theories
1. protiens
2. chaperones

Front 7

certain diseases are characterized by...

Back 7

extensive protein deposits in certain tissues

Hint 7

what diseases are characterized by

Front 8

alzheimer noted that...

Back 8

neurofibrilary tangles and neuritic plaaque (dieseases that have extensive nerve cell death) are specific to alzheimers

Hint 8

neurofibrilary tangles
neuritic plaque

Front 9

key to a-helix and b-sheet

Back 9

hydrogen bond

Hint 9

type of bond

Front 10

number of amino acids for each turn of the a-helix

Back 10

3.6 amino acids

Hint 10

decimal number

Front 11

a-helix

Back 11

right hand spiral stabilized by hydrogen bonds btwn each amino acid (nitrogen atom and the oxygen atom) of the fourth one up the chain

Hint 11

what type of spiral
what type of bonds
number up the chain

Front 12

b-sheet

parallel

antiparallel

Back 12

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

Hint 12

flat or round?
what sticks out
what type of bonds
definitions

Front 13

antiparallel sheets

b-turn

Back 13

often formed by one chain looping back on itself
b-turn- the 1 to 3 amino acids linking 2 strands

Hint 13

what does it do
definition

Front 14

partially folded chains

Back 14

fold in a fraction of a second

Hint 14

how long

Front 15

P22

Back 15

virus that infects bacteria

Hint 15

virus or bacteria?

Front 16

high temp. sensitive mutations

Back 16

one amino acid altered and turns into insoluble gunk, able to analyze bacterial cells to see what went wrong with the folding

Hint 16

whats altered
what happens at high temps
scientists analyze what

Front 17

FAP

Back 17

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

Hint 17

whats damaged by amyloid-type protein
rare or not rare disease?
what type of mutations
how many

Front 18

transthyretin aggregation

Back 18

monomeric unfolding intermediate

Hint 18

monomeric what

Front 19

transthyretin

Back 19

normal transthyretin, when protein is broken down it turns to insoluble gunk that poisons the tissues where it is deposited

Hint 19

normal what?
when protein breaks down what happens?

Front 20

alzheimers afflicts...

Back 20

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

Hint 20

what % over 65
what % over 85
kills how many each year
costs how much each year

Front 21

neuritic plaque

Back 21

pathway leading to alzheimers

Hint 21

pathway leading to what

Front 22

alzheimers disease is limited...

Back 22

to old people b/c the process takes a long time, have the normal amyloid precursor protein

Hint 22

what type of ppl and why
have normal what protein

Front 23

apoE

Back 23

trasports cholesterol and other fatty materials in the blood stream, rapid formation of plaque

Hint 23

transports what
rapid formation of what

Front 24

AB plays a major roll in __ disease

Back 24

alzheimers

Hint 24

what disease

Front 25

prions

Back 25

protein particles, pure protien that contain neither DNA or RNA, self replicating (own chaperone)

Hint 25

what type of particles
doestn contain what and what
what does it do (replicate)

Front 26

mad cow (scrapie, creutzfeldt-jacob)

Back 26

diseases transmitted by prions

Hint 26

transmitted by what

Front 27

cystic fibrosis

Back 27

lack of protein that regulates the transport of the chloride ion across the cell membrane

Hint 27

lack of what
regulates what across what

Front 28

cystic fibrosis hinders...

Back 28

seperation of the transport regulator protein from one of its chaperones, final steps in folding cant occur, normal amounts of active protein arent produced

Hint 28

seperation of what from what
final steps in what cant occur
normal amounts of what arent produced

Front 29

emphysema

Back 29

buildup of a crucial folding intermediate leads to aggregation which deprives some of enough circulating a1 antitrypsin to protect lungs

Hint 29

buildup of what
leads to what that deprives some of what al antitryspin to do what to the lungs

Front 30

purpose of studying diseases

Back 30

find ways to treat it

Hint 30

find ways to do what

Front 31

p53

Back 31

involved in 40% of all human cancers, prevents cells from becoming cancerous

Hint 31

what % of all cancers
prevents what

Front 32

p53 (2 clases)

Back 32

1.keeps protein from binding to DNA
2.makes folded form of protein less stable

Hint 32

1.keeps what from happening
2.makes what less stable

Front 33

TIP and the thyroid hormone

Back 33

can stabilize transthyretin and is a treatment for FAP

Hint 33

transthyretin
FAP

Front 34

once folding is complete...

Back 34

chaperone will leave its protein to help another

Hint 34

what a chaperone does once folings done

Front 35

how many chaperones can there be

Back 35

several

Hint 35

one or several?

Front 36

chaperones primary function

Back 36

prevent aggregation

Hint 36

to prevent what