Water accessibility to trypophan residues in horse apomyoglobin

Abstract

Water molecules are generally considered not to reach the buried hydrophobic center of proteins. A study on tryptophan residues embedded in the A, G, H helices cluster apomyoglobin shows that water molecules can access these residues. It is suggested that the arrival of water at the burried residues could result from the protein's specific flexibility, which is itself regulated by the solvation state of the protein surface.