Strength of the (CH)-H-alpha center dot center dot O hydrogen bond of amino acid residues

Although the peptide (CH)-H-alpha group has historically not been thought t o form hydrogen bonds within proteins, ab initio quantum calculations show it to be a potent proton donor. Its binding energy to a water molecule lies in the range between 1.9 and 2.5 kcal/mol for nonpolar and polar amino aci ds; the hydrogen bond (H-bond) involving the charged lysine residue is even stronger than a conventional OH . .O interaction. The preferred H-bond len gths are quite uniform, about 3.32 Angstrom. Formation of each interaction results in a downfield shift of the bridging hydrogen's chemical shift and a blue shift in the (CH)-H-alpha stretching frequency, potential diagnostic s of the presence of such an H-bond within a protein.