Explain how the three-dimensional structures of proteins enable enzymes to perform their functions as biological catalysts
The specific three-dimensional structure for an enzyme is highly important due to its reassembling of its active site. This can among other include that negatively charged amino acids has to be present near other specific amino acids in order to play a role in the catalytic mechanism. It could be the presence of a hydroxyl amino acid such as threonine and serine which are common amino acids used in catalysis. Another thing is that when we look at the protein in a native folded state versus its unfolded state, you can notice there is a lot more solvent exposure to some residues in the unfolded state compared to that in the native state. So simply the important of a hydrophobic core in a protein is also considered viral to enzyme activity, the reasons for this are multiple, but one very important effect of the hydrophobic core is that many of the charged amino acids will let their side chain pKa shift towards 7 (surely this is not always the case, a more general principle can be formulated).
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