Carugo O
Department of General Chemistry of the Pavia University, Italy.
Biol Chem. 1999 Apr;380(4):495-8. doi: 10.1515/BC.1999.064.
The stereochemical features of the interaction between the sulfur atom of methionine residues and surrounding atoms are examined on a large set of known protein crystal structures. It appears that the minimum energy conformations observed in small molecule crystals are not observed within the protein core. This suggests that these interactions are either of little intensity, though they might contribute to regulate the protein physiological behavior, or physicochemically different from their counterpart in small molecule crystals.
在大量已知的蛋白质晶体结构上，研究了甲硫氨酸残基的硫原子与周围原子之间相互作用的立体化学特征。结果表明，在小分子晶体中观察到的最低能量构象在蛋白质核心区域并未出现。这表明这些相互作用要么强度很小，尽管它们可能有助于调节蛋白质的生理行为，要么在物理化学性质上与小分子晶体中的对应相互作用不同。
