An alanine in the core of the protein is mutated to leucine. Referring to the LenardJones...
An alanine in the core of the protein is mutated to leucine. Referring to the LenardJones potential, briefly explain what effect this will have on the chemical potential of the folded state. Does the protein become more or less stable?
Homework Answers
Alanine is a hydrophobic amino acid and proteins structure is consist of interior core and external.
Interior is stable by hydrophobic( nonpolar) amino acids because of hydrophobic interactions. External is stable by various ionic interactions of polar amino acids or charged amino acids which cause interactions with water molecules which is polar.
So if Alanine is mutated and leucine is added, as leucine is more hydrophobic as it's hydrocarbon change is long than only hydrogen molecule is present.
So mutated protein will be more stable and it's potential will be more because if you want to change its conformation energy will be needed more.
Thank you
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An alanine in the core of the protein is mutated to leucine.
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globular protein to be stabilizing or destabilizing? Assume the
mutant folds to a native-like conformation. Explain your answer in
terms of the predicted enthalpic and entropic
effects of the mutation on the ΔG for protein folding compared to
ΔG of folding for the wild-type protein.
Match the items in the left column to the appropriate blanks in
the sentences on the right.
ASsolvent Because the mutation is on...
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please help me with this biochemestry question
An experiment was conducted to analyze the favorability of folding for a short polypeptide consisting entirely of alanine. This polypeptide folds favorably into a single, continuous a-helix. If an individual alanine residue in the polypeptide is changed to glycine, Delta G_ren for the folding of the a-helix increases by +1.88 kcal/mol. In which of the two peptides is a-helix assembly more favorable, the alanine-only peptide or the glycine-containing peptide? Briefly explain your answer....
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Pls answer fast
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