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25 Cards in this Set
- Front
- Back
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What are the major differences between a 310 helix and an alpha helix?
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310 helix: 3 residues per turn, 10 atoms per H-bond loop; alpha helix: 3.6 residues per turn, 13 atoms per H-bond loop
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What are the two main forces that stabilize an alpha helix?
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H-bonding; nucleophilic N-Pi star interaction
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How many classes of enzymes are there?
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6
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Name three classes of enzymes.
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hydrolase, isomerase, ligase
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Reverse inhibition that appears to decrease Km and Vmax proportionally
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Uncompetitive inhibition
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Reverse inhibition that appears to decrease Vmax without changing Km
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Noncompetitive inhibition
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Reverse inhibition that appears to change Km without changing Vmax
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Competitive inhibition
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The 3-D structure of proteins may be determined by ___ and ___.
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x-ray diffraction; NMR spectroscopy
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Oxygen binding to hemoglobin is characterized by positive ___ and ___ regulation.
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cooperativity; allosteric
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In proteins that contain quaternary structure, subunits are usually held together by ___ interactions.
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noncovalent
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The sequence of a polypeptide chain may be determined by the ___ procedure, in which N-terminal residues are successively cleaved.
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Edman degradation
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The major noncovalent interactions that determine the structures of biomolecules are ____ and ___.
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hydrophobic; electrostatic
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True or False: Collagen is formed from three right handed helices that form a left handed supercoil.
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False
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True or False: The variable domains of antibodies are at the end of the heavy and light chain and interact with the antigen.
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True
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After a protein is denatured with denaturing agents, it cannot be renatured.
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False
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The tertiary structure of a protein may be formed from the folding of independent subunits to form a homodimer.
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False
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Beta sandwiches are held together by hydrophobic forces.
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True
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A solution that contains equal, or nearly equal quantities of weak acid and its conjugate base is called a/an ___.
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buffer solution
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Within the hydrophobic interior of a protein, the attraction between two oppositely charged functional groups is often called a ___.
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salt bridge
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The pH at which a given amino acid carries a net zero charge is referred to as ___.
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the isoelectric point (pI)
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The covalent linkage formed by the oxidation of the side chains of two cysteine residues in a peptide or protein is called a/an ___.
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disulfide bridge
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The Bohr effect explains why hemoglobin has a ___ affinity for oxygen when levels of carbon dioxide and H+ are elevated.
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lower
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The predominant type of secondary structure seen in myoglobin is ___.
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alpha helix
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An organic molecule in erythrocytes that lowers the affinity of hemoglobin for oxygen is ___.
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2,3-BPG
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Scurvy is a condition arising from the inability to make functional collagen. This is caused by the absence of ___ which makes the formation of ___ impossible.
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vitamin C; hydroxyproline
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