A designed cavity in the hydrophobic core of a four-alpha-helix bundle improves volatile anesthetic binding affinity

A study was conducted on the structural features of protein binding sites for volatile anesthetics. The findings indicate that volatile general anesthetics in vivo may occupy packing defects present on natural proteins and that the di-alpha-helical peptides dimerize in an anti orientation. The results also verified the hydrophobic core location of the tryptophan and cysteine residues.