Events

Since the early work of Pauling and Corey, the paradigm for thinking about and modeling protein backbone geometry has been that of a single ideal set of bond lengths and angles for the peptide unit. Based on the crystallographically determined structures of proteins, I published work in the mid-90s showing that there is strong evidence for systematic variations in bond angles as a function of the conformational differences only involving rotations around single bonds. We are now surveying protein structures determined at <1 � resolution to better characterize the systematic variations.