Term
| How does SDS-Page separate proteins? |
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Definition
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Term
| In what type of chromatography, is a protein mixture applied to the column at a low pH so that the proteins will have a net positive change and bind to the column? |
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Definition
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Term
| In SDS-PAGE electrophoresis, disulfide-linked protein subunits are separated by first reacting them with what? |
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Definition
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Term
| The first step in purifying a protein that was initially associated with a fatty substance would be...? |
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Definition
| hydrophobic chromatography |
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Term
| What determines the length an amino acid takes to elute from an exchange column? (anion and cation, and what moves slower and slower on each) |
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Definition
Charge determines the speed of the elution.
For an Anion-exchange columnn positive charges move slower.
For a Cation-exchange column, negative charges move slower. |
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Term
| What causes the 'salting in' of proteins? |
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Definition
| hydration of the salt ions reducing solubility of proteins. |
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Term
| What type of protein is found in hair, horns, nails, and feathers? |
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Definition
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Term
| In a trans peptide bond, what is the dihedral angle? |
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Definition
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Term
| In a cis peptide bond, what is the dihedral angle? |
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Definition
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Term
| What conformations have both favorable hydrogen bonding patterns, and theta/omega values that fall withing the allowed Ramachandran conformational regions? |
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Definition
| alpha helix, collagen helix, and beta sheets. |
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Term
| An increase in pCO2 causes hemoglobin's affinity for oxygen to do what? |
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Definition
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Term
| What tier of structure are alpha helices, and beta sheets? |
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Definition
| Regular Secondary Structure. |
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Term
| What is found in bone, teeth, cartilage, and tendons? |
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Definition
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Term
| In the absence of ascorbic acid, prolyl oxidase is unable to oxidize proline residues in collagen to hydroxyproline, resulting in what? |
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Definition
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Term
| What determines if keratin is hard/soft? |
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Definition
| The proportion of proline residues. |
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Term
| Describe the structure of keratin. |
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Definition
| It consists of coiled-coil structures, which form dimers and then associate to form protofilaments. |
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Term
| What gives keratin its springiness? |
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Definition
| The coiled-coil structures. |
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Term
| What is a triple-helical fibrous protein? |
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Definition
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Term
| In Sickle Cell, hemoglobin does form fibers in what form? |
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Definition
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Term
| What non-covalent forces stabilize protein structure? |
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Definition
| The hydrophobic effect, salt bridges, metal-ion coordination, and hydrogen bonding. |
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Term
| Protein diseases are caused by? |
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Definition
| Mutations affecting the primary structure. |
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Term
| In what way does hemoglobin's subunits bind to oxygen? |
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Definition
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Term
| The absence of 2,3-BPG causes hemoglobin's affinity for oxygen to do what? |
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Definition
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Term
| What is the functions of SDS in SDS-PAGE? |
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Definition
| to denature/unfold the protein |
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Term
| What happens when unstable hemoglobin are degraded, leading to cell lysis? |
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Definition
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Term
| When the partial pressure of oxygen is venous blood is 30 torr, the Y02 value for myoglobin/hemoglobin are respectively? |
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Definition
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Term
| What are the ligands to the Fe2+ ion of the porphyrin ring in oxymyoglobin? |
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Definition
| His E7, His F8, Nitrogen atoms in the porphyrin ring, and oxygen. |
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Term
| What is Myoglobin's secondary structure primarily composed of? |
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Definition
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Term
| Hemoglobin's P50 value is how many times as great as myoglobin's P50 value? |
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Definition
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Term
| What increase the affinity or hemoglobin for oxygen? |
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Definition
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Term
| The fastest way that erythrocytes adapt to high altitude is? |
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Definition
| By increasing the intracellular concentration of BPG. |
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Term
| If the binding of O2 to hemoglobin what characterized by a Hill constant of -1, what would this imply? |
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Definition
| That hemoglobin would not be able to release bound O2. |
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Term
| Digestion of the IgG molecule with enzyme papain produces which of the following fragments? |
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Definition
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Term
| If two proteins are isoelectric at the same pH, at what pH should the be separated by electrophoresis? |
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Definition
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Term
| What are 4 characteristics of the alpha-helix? |
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Definition
| Proline is typically not found in the alpha helix, there are 3.6 amino acids per turn, a hydrogen bond forms between the carobonyl oxygen of the nth amino acid residue and the NH group of the (n+4)th amino acid residue, and it is right-handed. |
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Term
| What is the average distance between the pleats of a parallel beta sheets? |
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Definition
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Term
| In helix nomenclature, what does the number mean? What does the subscript mean? |
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Definition
| The number means the number of atoms, and the subscript stands for the number of amino acids in the loop. |
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Term
| The binding of 2.3-bisphosphoglycerate to hemoglobin can best be described by what? |
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Definition
One BPG binds to each deoxygenated subunit of hemoglobin.
It promotes the release of oxygen from hemoglobin.
It contains two phosphate groups.
It causes increased ionic bonding between subunits. |
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Term
| In what form of hemoglobin, is the iron ion in the same plane as the porphyrin ring? |
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Definition
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Term
| In sicle-cell anemia, what amino acid is replaced with what? |
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Definition
| Negative Glutamic Acid, is replaced with the neutral Valine. |
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Term
| When do proteins normally exhibit minimum solubility in aqueous solution? |
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Definition
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Term
| What are 4 properties of the glycine and collagen helix? |
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Definition
Glycine stabilizes the mature collagen fiber by its participation in covalent cross-link formation.
Glycine is tolerated in the collagen helix because of the small size of its side group.
Glycine stabilizes the collagen helix by hydrogen-bonding.
glycine accounts for about one third of the amino acid composition of collagen. |
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Term
| What type of curve does the binding of O2 to hemoglobin as a function of pO2 exhibit? |
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Definition
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Term
| The binding of myoglobin can be described as what kind of curve? |
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Definition
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Term
| How does how high altitudes effect 2,3-BPG concentrations in the blood? |
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Definition
| the concentration increases. |
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Term
| What happens with an increased level of 2,3-BPG? |
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Definition
| More oxygen is released from hemoglobin |
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Term
| The omega angle of a peptide bond is described by rotation about the bond...? |
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Definition
| that is between the Calpha and C atoms. |
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Term
| What is the chemical entity that provides the energy for the movement of myosin heads to striated muscle cells? |
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Definition
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Term
| What type of Hill coefficient indicated that a hemoglobin's ability to bind to oxygen has been compromised? |
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Definition
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Term
| What is the Bohr effect related to? |
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Definition
| The ability of hemoglobin to bind to oxygen in the presence of BPG. |
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Term
| In the contraction cucle of myosin molecules as they walk along thin filaments in striated muscle cells binding of ATP results in, what? |
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Definition
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Term
| Which residues in the seven-residue repeat (abcdefg) of alpha-keratin provide a mechanism by which keratin polymers associate to form a coiled coil? |
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Definition
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