3.5 An a helical, intracellular protein, ITSME, denatures at 80 degrees Celsius. Which of the following are true about ITSME? Above 80 degrees Celsius, disulfide bonds break, destabilizing the protein. Mutating 2 residues in an a helical part of ITSME to proline will likely decrease the temperature at which ITSEME denatures. At temperatures below 80 degrees Celsius, ITSME adopts a folded structure largely due to the hydrophobic effect. Increasing temperature provides sufficient kinetic energy to overcome the very large free energy difference between the folded and unfolded states of ITSME.
3.5 An a helical, intracellular protein, ITSME, denatures at 80 degrees Celsius. Which of the following are true about ITSME? Above 80 degrees Celsius, disulfide bonds break, destabilizing the protein. Mutating 2 residues in an a helical part of ITSME to proline will likely decrease the temperature at which ITSEME denatures. At temperatures below 80 degrees Celsius, ITSME adopts a folded structure largely due to the hydrophobic effect. Increasing temperature provides sufficient kinetic energy to overcome the very large free energy difference between the folded and unfolded states of ITSME.
Biochemistry
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ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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Transcribed Image Text:3.5 An a helical, intracellular protein, ITSME, denatures at 80 degrees Celsius. Which of the
following are true about ITSME?
Above 80 degrees Celsius, disulfide bonds break, destabilizing the protein.
Mutating 2 residues in an a helical part of ITSME to proline will likely decrease the
temperature at which ITSEME denatures.
At temperatures below 80 degrees Celsius, ITSME adopts a folded structure largely due
to the hydrophobic effect.
Increasing temperature provides sufficient kinetic energy to overcome the very large
free energy difference between the folded and unfolded states of ITSME.
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