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