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Unformatted text preview: (2) (3) (4) CIRCLE ONE! 8 Question #7 (4 points)
In the organic solvent dioxane, an amino acid chain composed entirely of leucine adopts an α-helical
conformation however one composed entirely of isoleucine adopts a “random coil conformation.” Explain the
reason for this. The term “random coil” is used by protein biochemists to refer to a conformation lacking any
recognizable repetitive structure.
O = Dioxane
O Question #8 (9 points) True (T) or False (F)? The hydrophobic effect refers to the stabilization of protein structure due to H-bonds
between the hydrophobic side chains of amino acyl residues. ________ During polypeptide folding, the number of H-bonds formed is much larger than
than the number broken. ________ As compared to the unfolded state, the folded state of a polypeptide is highly stable one. ________ β-mercaptoethanol denatures proteins by disrupting internal H-bonds. ________ Anionic detergents are expected to be more effective denaturants than uncharged ones. ________ Motionally restricted water molecules surrounding oligomeric proteins stabilize
. ________ When a polypeptide folds, most hydrophilic groups of the peptide linkage maintain
H-bonds with water. ________ A polypeptide folds spontaneously with a ∆HFOLD = 0
This means that T∆SWATER must be > T∆SPOLY . ________ A protein with a low % content of α-helix tends...
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This test prep was uploaded on 04/01/2014 for the course BIOL 201 taught by Professor Chowrira during the Winter '13 term at UBC.
- Winter '13