Biology, asked by Shiva1086, 1 year ago

What is the impact of hydrophobicity of small molecule on ligand-protein interaction

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Answered by Anonymous
10

Together, these results show that fragments are using polar interactions to gain maximum binding efficiency from a limited number of interactions, but as small-molecule ligands are optimized, geometric constraints associated with polar bonds are more challenging to satisfy, and the contribution of hydrophobic

Answered by Anonymous
0

Together, these results show that fragments are using polar interactions to gain maximum binding efficiency from a limited number of interactions, but as small-molecule ligands are optimized, geometric constraints associated with polar bonds are more challenging to satisfy, and the contribution of hydrophobic

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