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29 Cards in this Set
- Front
- Back
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What is craniopharyngioma? What results from it? How was this treated in the early 80's?
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Benign brain tumor that leads to panhypopituitarism (lack HGF)
Injected with HGF from cadavers |
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Describe the Central Paradigm (Dogma) of Molecular Biology.
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DNA-->RNA : Transcription
RNA--> Protein: Translation Protein-->Function |
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In what ways can protein function be regulated?
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Rate of gene transcription (mRNA production)
RNA splicing RNA degradation (stability) Rate of translation Rate of protein degradation Transport of protein to final location Post-translational mods |
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What is the general structure of an amino acid?
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NH2-CH(R)-CO2H
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Where are non-polar amino acids found?
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Interior of water-soluble proteins; surface of lipid-soluble proteins
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Where are uncharged polar amino acids found?
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Interior of lipid-soluble proteins, surface of water-soluble proteins
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Where are acidic amino acids found?
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Interior of lipid-soluble proteins, surface of water-soluble proteins
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Where are basic amino acids found?
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Interior of lipid-soluble proteins, surface of water-soluble proteins
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Which amino acids are considered non-polar?
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Alanine
Glycine Isoleucine Methionine Phenylalanine Proline Tryptophan Valine |
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Which amino acids are considered uncharged polar?
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Asparagine
Cysteine Glutamine Serine Threonine Tyrosine |
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Which amino acids are considered acidic?
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Aspartic acid
Glutamic acid |
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Which amino acids are considered basic?
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Arginine
Histidine Lysine |
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What determines the charge of the side chains of acidic and basic amino acids at physological pH?
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pK as dictated be H-H eqn
just think of pH= pKa + log A-/HA and compare relative to each other |
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How are peptide bonds formed? What kinds of bonds are they? How can they be broken?
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Condensatino reaction; covalent bond; require protease
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What is special about proline?
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non-polar side chain in form of a ring structure; this interrupts alpha-helices
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What's special about cysteine?
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uncharged polar side chain; can form disulphide bonds
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What are the key features of protein phosphorylation?
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It is REVERSIBLE
Phosphorylation catazlyed by Kinases Dephosphorylation catalyzed by Phosphatases Phosphate donor is almost always ATP Phosphorylation is a post-translational modification and can allow for rapid change in shape and function Addition of phosphate usually adds to serine or threonine or tyrosine |
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How can protein phosphorylation be regulated?
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Kinase can be regulated
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Which form of amino acids (L or D) used in proteins?
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L
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Why do polypeptides assume permanent configurations?
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Peptide bonds behaves like a partial double bond, so will not rotate. Configuration is defined.
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What is the primary structure of a protein?
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amino acid sequence (written N-->C)
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What is a protein's secondary structure? What allows for it?
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H-bonds between side groups of adjacent amino acids result in:
alpha-helix (right-handed) beta-sheet (N--->C): can be parallel or anti-parallel can also have beta-bends, loops, coils, barrels, etc... |
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What is a protein's tertiary structure?
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H-bonding between non-adjacent aa's resulting in folding/arrangement of domains
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What is a protein's quaternary structure?
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Interactions between separate proteins
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What is protein denaturation? How can it be achieved?
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Unfolding and disorganization of a protein
heat, organic solvens, changes in pH (addition of acids/bases), detergents, heavy metals; these can change charge of side groups, or affect IMF's, which affect folding |
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What role do chaperones play? Give an example.
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Assist in protein folding; ex: heat-shock proteins (high levels of these when temp goes up)
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How do amyloidoses arise? What disease are they involved in?
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Primary gene mutation alters primary structure of a protein such that it doesn't fold correctly. One amyloidose is AD.
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What is prion disease? Give examples.
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Abnormal version of a protein (very stable; misfolded) can interact with proteins they'd normally associate with and produce more misfolded proteins; takes years to accumulate misfolded proteins.
Ex: Creutzfeldt-Jacobs, mad cow dz |
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Which amino acids have polar hydroxyl groups? Why is this of importance?
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Serine, Threonine, Tyrosine
Can accept phosphate groups, which can be acted upon my kinases (post-translational mod) |
