Specific rotation is a measure of a solution's capacity to rotate circularly polarized light. The unfolding of the a helix of a polypeptide to a random conformation is accompanied by a large decrease in specific rotation. Polyglutamate, a polypeptide made up of only 1-Glu residues, has the a helix conformation at pH 3. When researchers raise the pH to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (1.-Lys residues) is an a helix at pH 10, but when researchers lower the pH to 7 the specific rotation also decreases, as shown in the graph. a Helix Specific rotation Poly(Glu) a Helix Random conformation Poly(Lys) Random conformation T + ° 2 4 6 В 10 12 14 PH Complete the statements about the molecular mechanism for these changes in specific rotation. Increasing the pH of a polyglutamate solution from 6 to 7 causes the carboxyl group of each glutamate residue Comed Artwer lose a proton. The negatively charged groups in each glutamate residue Comet A leading to unfolding of the a helix. Come Awar repel each other, Correct A Decreasing the pH of a polytysine solution from 9 to 7 causes the amino group of each lysine residue to Coed Ar gain a proton The Come Awe unfolding of the helix. positively charged groups in each lysine residue Come A repel Comed Anwe each other, leading to
Specific rotation is a measure of a solution's capacity to rotate circularly polarized light. The unfolding of the a helix of a polypeptide to a random conformation is accompanied by a large decrease in specific rotation. Polyglutamate, a polypeptide made up of only 1-Glu residues, has the a helix conformation at pH 3. When researchers raise the pH to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (1.-Lys residues) is an a helix at pH 10, but when researchers lower the pH to 7 the specific rotation also decreases, as shown in the graph. a Helix Specific rotation Poly(Glu) a Helix Random conformation Poly(Lys) Random conformation T + ° 2 4 6 В 10 12 14 PH Complete the statements about the molecular mechanism for these changes in specific rotation. Increasing the pH of a polyglutamate solution from 6 to 7 causes the carboxyl group of each glutamate residue Comed Artwer lose a proton. The negatively charged groups in each glutamate residue Comet A leading to unfolding of the a helix. Come Awar repel each other, Correct A Decreasing the pH of a polytysine solution from 9 to 7 causes the amino group of each lysine residue to Coed Ar gain a proton The Come Awe unfolding of the helix. positively charged groups in each lysine residue Come A repel Comed Anwe each other, leading to
Human Heredity: Principles and Issues (MindTap Course List)
11th Edition
ISBN:9781305251052
Author:Michael Cummings
Publisher:Michael Cummings
Chapter9: Gene Expression And Gene Regulation
Section: Chapter Questions
Problem 19QP: Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the...
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Transcribed Image Text:Specific rotation is a measure of a solution's capacity to rotate circularly polarized light. The unfolding of the a helix of a
polypeptide to a random conformation is accompanied by a large decrease in specific rotation.
Polyglutamate, a polypeptide made up of only 1-Glu residues, has the a helix conformation at pH 3. When researchers raise the
pH to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (1.-Lys residues) is an a helix at pH
10, but when researchers lower the pH to 7 the specific rotation also decreases, as shown in the graph.
a Helix
Specific rotation
Poly(Glu)
a Helix
Random
conformation
Poly(Lys)
Random conformation
T
+
°
2
4
6 В
10 12 14
PH
Complete the statements about the molecular mechanism for these changes in specific rotation.
Increasing the pH of a polyglutamate solution from 6 to 7 causes the carboxyl group of each glutamate residue
Comed Artwer
lose a proton. The negatively charged groups in each glutamate residue
Comet A
leading to unfolding of the a helix.
Come Awar
repel
each other,
Correct A
Decreasing the pH of a polytysine solution from 9 to 7 causes the
amino
group of each lysine residue to
Coed Ar
gain a proton
The
Come Awe
unfolding of the helix.
positively charged groups in each lysine residue
Come A
repel
Comed Anwe
each other, leading to
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