Question

1. Interpret the data - Factors that affect protein folding Extreme conditions can cause a protein to partially (or even completely) unfold. Once normal conditions are restored, some proteins, like the digestive enzymes ribonuclease A and lysozyme, can refold. Ribonuclease A, natural form Denaturation Renaturation Ribonuclease A, denatured form The following figure and caption are modified from a scientific paper published in 1957 describing a study on how important disulfide linkages are to ribonuclease denaturation and renaturation (refolding). ACTIVITY 100 75 50 25 0 2 4 6 8 SH GROUPS Fig. 1. Activity of ribonuclease at various stages of reduction (expressed as percentage of the specific activity of native ribonuclease) as a function of the number of moles of sulfhydryl per mole of enzyme. ?, ?, Reduction ?, ?, ?, Reoxidation of fully reduced, inactive ribonuclease Reprinted with permission from AAAS ... Examine the image above and complete the following three items: What is the activity of a ribonuclease molecule that has no sulfhydryl (-SH) groups? Based on the data above, what is the maximum number of disulfide linkages found in a molecule of native (natural) ribonuclease? The number of free sulfhydryl groups in ribonuclease decreases as the protein undergoes a chemical process called oxidation. Therefore, oxidation causes ribonuclease to undergo denaturation refolding.

          1. Interpret the data - Factors that affect protein folding
Extreme conditions can cause a protein to partially (or even completely) unfold. Once normal conditions are restored,
some proteins, like the digestive enzymes ribonuclease A and lysozyme, can refold.
Ribonuclease A, natural form
Denaturation
Renaturation
Ribonuclease A, denatured form
The following figure and caption are modified from a scientific paper published in 1957 describing a study on how
important disulfide linkages are to ribonuclease denaturation and renaturation (refolding).
ACTIVITY
100
75
50
25
0 2 4 6 8
SH GROUPS
Fig. 1. Activity of ribonuclease at various stages of reduction (expressed as percentage of the specific activity of native ribonuclease) as a function of the number of moles of sulfhydryl per mole of enzyme.
?, ?, Reduction
?, ?, ?, Reoxidation of fully reduced, inactive ribonuclease
Reprinted with permission from AAAS ...
Examine the image above and complete the following three items:
What is the activity of a ribonuclease molecule that has no sulfhydryl (-SH) groups?
Based on the data above, what is the maximum number of disulfide linkages found in a molecule of native (natural) ribonuclease?
The number of free sulfhydryl groups in ribonuclease decreases as the protein undergoes a chemical process called oxidation. Therefore, oxidation causes ribonuclease to undergo denaturation refolding.

1. Interpret the data - Factors that affect protein folding
Extreme conditions can cause a protein to partially (or even completely) unfold. Once normal conditions are restored,
some proteins, like the digestive enzymes ribonuclease A and lysozyme, can refold.
Ribonuclease A, natural form
Denaturation
Renaturation
Ribonuclease A, denatured form
The following figure and caption are modified from a scientific paper published in 1957 describing a study on how
important disulfide linkages are to ribonuclease denaturation and renaturation (refolding).
ACTIVITY
100
75
50
25
0 2 4 6 8
SH GROUPS
Fig. 1. Activity of ribonuclease at various stages of reduction (expressed as percentage of the specific activity of native ribonuclease) as a function of the number of moles of sulfhydryl per mole of enzyme.
?, ?, Reduction
?, ?, ?, Reoxidation of fully reduced, inactive ribonuclease
Reprinted with permission from AAAS ...
Examine the image above and complete the following three items:
What is the activity of a ribonuclease molecule that has no sulfhydryl (-SH) groups?
Based on the data above, what is the maximum number of disulfide linkages found in a molecule of native (natural) ribonuclease?
The number of free sulfhydryl groups in ribonuclease decreases as the protein undergoes a chemical process called oxidation. Therefore, oxidation causes ribonuclease to undergo denaturation refolding.

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