A β-pleated sheet, contained within a globular protein, has two parallel strands connected by a turn....
A β-pleated sheet, contained within a globular protein, has two parallel strands connected by a turn. The turn is called a “beta-alpha-beta” motif. The α-helical portion (the turn) consists of 34 amino acids. The molecular weight of the entire sheet (including the α-helix) is 9.7 kd. What is the approximate length (i.e., the longest dimension) of this β-pleated sheet? Assume that the α-helix does not contribute to the length of the β-pleated sheet. (HINT: Since the amino acids in this particular α-helix do NOT have the typical “rise” that is seen commonly in this secondary structure, do NOT use the α-helical portion of this structure to calculate length.) (5 points)
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A β-pleated sheet, contained within a globular protein, has two
parallel strands connected by a turn....
(2%) Indicate which secondary structure or structures (α -helix, β -pleated, random coil) will the following...
(2%) Indicate which secondary structure or structures (α -helix,
β -pleated, random coil) will the following peptide adopt in an
aqueous solution at pH 7
(2%) The unfolding of the alpha helix of a polypeptide to a
randomly coiled conformation is accompanied by a large decrease in
a property called specific rotation, a measure of
a solution’s capacity to rotate circularly polarized light.
Polyglutamate, a polypeptide made up of only L-Glu residues, has
the alpha helical
conformation at pH 3....
(2%) Indicate which secondary structure or structures (α -helix,
β -pleated, random coil) will the following peptide adopt in an
aqueous solution at pH 7
(2%) The unfolding of the alpha helix of a polypeptide to a
randomly coiled conformation is accompanied by a large decrease in
a property called specific rotation, a measure of
a solution’s capacity to rotate circularly polarized light.
Polyglutamate, a polypeptide made up of only L-Glu residues, has
the alpha helical
conformation at pH 3....
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