How do bacteria distinguish enantiomers?
Bacteria can distinguish enantiomers because the enzymes in bacteria are chiral.
Bacteria release enzymes to break down substances, and these enzymes consist of amino acids.
Amino acids are chiral. So the receptor sites on the enzymes have a specific shape that fits one enantiomer of a substrate much better than the other.
One enantiomer then undergoes an enzyme-catalyzed reaction much faster than the other.
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Bacteria can distinguish enantiomers through specific enzymes or receptors that interact differently with the molecules' spatial arrangements. These enzymes or receptors have active sites that can only accommodate one enantiomer, leading to selective binding and recognition.
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When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.
When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.
When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.
When evaluating a one-sided limit, you need to be careful when a quantity is approaching zero since its sign is different depending on which way it is approaching zero from. Let us look at some examples.
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