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If we mix a protein (P) and its ligand (L) and allow the binding reaction to come to equilibrium (P+LßàPL), the formula [P][L]/[PL] = Kd can be used to determine the dissociation constant. Several weak, noncovalent bonds form between the protein and ligand when they bind. What would be the consequence of a mutation in the protein that did not disrupt its normal structure but prevented its ability to form one hydrogen bond with the ligand?No binding would occur and the Kd would be very low[P] and [L] would increase at equilibrium and the Kd would increase[P] and [L] would increase at equilibrium and the Kd would decrease[PL] would increase at equilibrium and the Kd would decrease

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