Question 20 of 23 Map Sapling Learning macmillan learning Consider the hypotheti
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Question 20 of 23 Map Sapling Learning macmillan learning Consider the hypothetical serine protease below, which shows the specificity pockets. The S1 pocket hasa glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S1' pocket is deep and hydrophobic. Suggest an amino acid sequence that this protease would cleave Which of the following sequences would this protease cleave? O Gly-Lys-Leu O Leu-Lys-Gly O Leu-Gly-Lys O Lys-Leu-Gly O Gly-Leu-Lys O Lys-Gly-Leu Previous ? Give Up & View Solution Check Answer ? Next Exit HintExplanation / Answer
According to the question the S1 pocket has a glutamic acid in the bottom. We all know that the glutamic acid is a negatively charged amino acid. So, the pocket is hydrophilic and can bind easily to the positively charged lysine. The middle amino acid of the sequence is lysine (Lys). So, the first two options are accepted and the remaining options are rejected.
The S2 pocket is small and hydrophobic. So this pocket is ready to bind/accommodate with the amino acid glycine (Gly) as glycine has a hydrogen atom as side chain.
The S1' pocket is deep and hydrophobic. So it is ready to bind/accommodate with leucine (Leu) as it has a larger side chain.
So the sequence of amino acid is Gly-Lys-Leu.
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