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51 Cards in this Set

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  • Back
  • 3rd side (hint)
name the 4 levels of protein structure:
primary
secondary
tertiary
quaternary
None
identify this protein structure: linear sequence of amino acids held together by peptide bonds
primary
protein primary sequence (determines/does not determine) the way a protein will fold into a unique three-dimensional.
determines
the 2 main forms of protein secondary structure are:
alpha-helix and beta-sheet
None
identify this protein structure: repeating structural elements produced through the hydrogen bonding of molecules in the peptide backbone itself
secondary
identify this protein structure: folding pattern of the secondary structural elements into a three-dimensional conformation
tertiary
the proteins tertiary structure is designed to serve all aspects of the protein’s function which are:
a.
b.
c.
binding sites
cellular localization
catalytic sites
None
protein folding begins at the … while the … is still being synthesized by the ribosome
N-terminus
C-terminus
None
interactions between amino acid … result in protein folding
side chains
in protein folding, where will you find hydrophobic side chains
tightly packed in core of protein
most charged and polar side chains are exposed … of the protein
on the surface
chaperones or charperonins are also known as …
heat shock proteins
name 2 heat shock proteins:
Hsp70 and Hsp60
heat shock proteins function to …
aid protein folding
what do heat shock proteins require to aid in the folding of proteins?
ATP
aside from heat shock proteins, what other 2 proteins involved in protein folding did we discuss in class?
cis-trans isomerases
protein disulfide isomerases (PDI)
None
where would one find cis-trans isomerases and
protein disulfide isomerases (PDI)
found in the RER
None
what is porteopathy?
abnormal accumulation (and resulting toxicity) of proteins in certain disease states
what is another name for protein conformational disease?
proteopathy
a misfolded protein has a tendency to polymerize into … that are resistant to clearance and can become ...
aggregates
pathogenic
None
name the 7 risk factors for proteopathy:
1.
2.
3.
4.
5.
6.
7.
1. increase in β-sheet secondary structure
2. mutations
3. abnormal post-translational modifications
4. changes in temperature and pH
5. increase in protein production
6. decrease in protein clearance
7. advancing age
None
what is the major aggregating protein in Alzheimer’s Disease
β -amyloid peptide (Aβ)
tau protein
None
what is the major aggregating protein in prion disease?
prion protein (may be infectious)
what is the major aggregating protein in Parkinson’s disease?
α-synuclein
what is the major aggregating protein in Huntington’s disease, triplet repeat disorders
proteins with tandem glutamine expansions
what is the major aggregating protein in type II diabetes
Islet amyloid polypeptide (IAPP or amylin)
what is the major aggregating protein in cataracts
crystallins
what is the major aggregating protein in various forms of amyloidosis
amyloid proteins, apolipoproteins, fibrinogen, lysozyme, ANF, keratin
identify this protein structure: present in proteins with multiple subunits
quaternary
what are the advantages of quaternary protein structure?
increased stability, cooperative binding, high affinity binding
what kind of bonds may be inolved in quaternary protein structures?
hydrogen binding
hydrophobic interactions
covalent (disulfide bonds)
None
as each O2 molecule binds to a hemoglobin subunit, the next subunit has increased affinity to bind O2, what does this describe?
positive coopertivity
how many subunits are there in hemoglobin and name them:
4
2 identical alpha chains and 2 identical beta chains
None
name the amino acid substitution in sickle cell anemia:
glutamic acid (glu) is replaced by valine (val)v in the 6th position in the beta chains
the mutated sickle cell hemoglobin is referred to as …
hemoglobin s
... becomes altered in sickle cell hemoglobin and ... remains unchainged?
solubility
O2 binding
None
what can happen to the red blood cells in sickle cell patients Under conditions of low oxygen?
polymerization and formation of fibrous precipitates that can damage rbc membranes, and can cause the cells to become stuck in blood vessels
how can hemoglobin s protect against malaria?
lysis of rbc's before plasmodium has chance to reproduce
immunoglobulins are proteins that are composed of … chains and … chains
2 light
2 heavy
None
keratin is the main constituent of structures that grow from the skin and is composed up mostly of … and … amino acids because they are the smallest of the amino acids which allows sterically-unhindered … bonds.
glycine
alanine
hydrogen
None
human hair is approximately 14% …
cysteine
disulfide bonding contributes to the ... of keratins
insolubility
what are the 3 steps to permanent hair waving?
1. Break the disulfide bonds with a reducing agent (ammonium hydroxide)
2. Shape the hair
3. Reform the disulfide bonds in new positions, using an oxidizing agent like hydrogen peroxide
None
protein unfolding is also known as …
denaturation
what can cause protein denaturation?
a.
b.
c.
d.
e.
a. nonenzymatic modification
b. high temperature
c. high concentrations of urea
d. extremes of pH
e. solvents that disrupt bonds
None
enzymes and other proteins will begin denaturing at temperatures between …
104°F - 106°F
… regulates our body temperature
hypothalamus
in cases of severe infections with dangerously high fevers, proteins may begin to …
unfold and lose their function
glycosylation of hemoglobin is due to …
sustained high glucose levels
… can be used as a valuable indicator of blood glucose levels over an extended period of time
glycosylated hemoglobin (HbA1C)
in protein folding, ... and ... groups of the peptide backbone maximize their potential to form ... with other backbone atoms
amide
carboxyl
hydrogen bonds