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A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be that
- a)the % helical content will decrease and % random conformation will increase.
- b)the % helical content will increase and % random conformation will decrease.
- c)there will be a transition from α-helix to β- sheet.
- d)there will be a transition from α-helix to β-hairpin.
Correct answer is option 'B'. Can you explain this answer?
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A 26-residue peptide composed of alanine and leucine shows circular di...
If a 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of αhelix at 50°C in 5 mM phosphate buffer at pH 7.4. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, then the % helical content will increase and % random conformation will decrease
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A 26-residue peptide composed of alanine and leucine shows circular di...
Explanation:
Effect of Temperature on Protein Conformation:
- As the peptide solution is cooled from 50°C to 25°C, the helical content of the peptide is expected to increase.
- This is because lower temperatures stabilize the α-helix conformation due to hydrogen bond formation.
Stabilization of α-Helix at Lower Temperatures:
- At 25°C, the peptide is more likely to adopt a more structured conformation, favoring the α-helical content.
- The gradual decrease in temperature promotes the formation and stability of α-helices in the peptide.
Shift from Random Conformation:
- The random coil conformation is less stable compared to the α-helix.
- Therefore, as the temperature decreases, the peptide is more likely to transition from the random coil to the α-helical conformation.
Summary:
- The most likely observation when the peptide solution is cooled gradually to 25°C is that the % helical content will increase, while the % random conformation will decrease.
- This transition is a result of the stabilization of the α-helical structure at lower temperatures.
Effect of Temperature on Protein Conformation:
- As the peptide solution is cooled from 50°C to 25°C, the helical content of the peptide is expected to increase.
- This is because lower temperatures stabilize the α-helix conformation due to hydrogen bond formation.
Stabilization of α-Helix at Lower Temperatures:
- At 25°C, the peptide is more likely to adopt a more structured conformation, favoring the α-helical content.
- The gradual decrease in temperature promotes the formation and stability of α-helices in the peptide.
Shift from Random Conformation:
- The random coil conformation is less stable compared to the α-helix.
- Therefore, as the temperature decreases, the peptide is more likely to transition from the random coil to the α-helical conformation.
Summary:
- The most likely observation when the peptide solution is cooled gradually to 25°C is that the % helical content will increase, while the % random conformation will decrease.
- This transition is a result of the stabilization of the α-helical structure at lower temperatures.
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A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be thata)the % helical content will decrease and % random conformation will increase.b)the % helical content will increase and % random conformation will decrease.c)there will be a transition from α-helix to β- sheet.d)there will be a transition from α-helix to β-hairpin.Correct answer is option 'B'. Can you explain this answer?
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A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be thata)the % helical content will decrease and % random conformation will increase.b)the % helical content will increase and % random conformation will decrease.c)there will be a transition from α-helix to β- sheet.d)there will be a transition from α-helix to β-hairpin.Correct answer is option 'B'. Can you explain this answer? for Software Development 2025 is part of Software Development preparation. The Question and answers have been prepared according to the Software Development exam syllabus. Information about A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be thata)the % helical content will decrease and % random conformation will increase.b)the % helical content will increase and % random conformation will decrease.c)there will be a transition from α-helix to β- sheet.d)there will be a transition from α-helix to β-hairpin.Correct answer is option 'B'. Can you explain this answer? covers all topics & solutions for Software Development 2025 Exam. Find important definitions, questions, meanings, examples, exercises and tests below for A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be thata)the % helical content will decrease and % random conformation will increase.b)the % helical content will increase and % random conformation will decrease.c)there will be a transition from α-helix to β- sheet.d)there will be a transition from α-helix to β-hairpin.Correct answer is option 'B'. Can you explain this answer?.
A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be thata)the % helical content will decrease and % random conformation will increase.b)the % helical content will increase and % random conformation will decrease.c)there will be a transition from α-helix to β- sheet.d)there will be a transition from α-helix to β-hairpin.Correct answer is option 'B'. Can you explain this answer? for Software Development 2025 is part of Software Development preparation. The Question and answers have been prepared according to the Software Development exam syllabus. Information about A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be thata)the % helical content will decrease and % random conformation will increase.b)the % helical content will increase and % random conformation will decrease.c)there will be a transition from α-helix to β- sheet.d)there will be a transition from α-helix to β-hairpin.Correct answer is option 'B'. Can you explain this answer? covers all topics & solutions for Software Development 2025 Exam. Find important definitions, questions, meanings, examples, exercises and tests below for A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be thata)the % helical content will decrease and % random conformation will increase.b)the % helical content will increase and % random conformation will decrease.c)there will be a transition from α-helix to β- sheet.d)there will be a transition from α-helix to β-hairpin.Correct answer is option 'B'. Can you explain this answer?.
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A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be thata)the % helical content will decrease and % random conformation will increase.b)the % helical content will increase and % random conformation will decrease.c)there will be a transition from α-helix to β- sheet.d)there will be a transition from α-helix to β-hairpin.Correct answer is option 'B'. Can you explain this answer?, a detailed solution for A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be thata)the % helical content will decrease and % random conformation will increase.b)the % helical content will increase and % random conformation will decrease.c)there will be a transition from α-helix to β- sheet.d)there will be a transition from α-helix to β-hairpin.Correct answer is option 'B'. Can you explain this answer? has been provided alongside types of A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be thata)the % helical content will decrease and % random conformation will increase.b)the % helical content will increase and % random conformation will decrease.c)there will be a transition from α-helix to β- sheet.d)there will be a transition from α-helix to β-hairpin.Correct answer is option 'B'. Can you explain this answer? theory, EduRev gives you an
ample number of questions to practice A 26-residue peptide composed of alanine and leucine shows circular dichroism (CD) spectrum characteristic of α-helix at 50°C in 5 mM phosphate buffer at pH 7.4. Deconvolution of the spectrum indicates 60% α-helical and 40% random conformation. When the peptide solution is cooled gradually to 25°C, and the CD spectra are recorded at different temperatures, the most likely observation will be thata)the % helical content will decrease and % random conformation will increase.b)the % helical content will increase and % random conformation will decrease.c)there will be a transition from α-helix to β- sheet.d)there will be a transition from α-helix to β-hairpin.Correct answer is option 'B'. Can you explain this answer? tests, examples and also practice Software Development tests.
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