Analysis of Backbone Hydrogen Bonding in a β-Turn of Staphylococcal Nuclease

摘要

The decreased energetic contribution of the α-helical hydrogen bonds relative to those in a β-sheet or β-turn may be a result of increased solvent accessibility to the α-helic dipole. Altogether, these studies suggest that backbone hydrogen-bonding interactions in the three major secondary structures commonly found in protein structures can contribute significantly to the overall stability of proteins.