Professor Krimm's research group has two main goals: developing infrared and Raman spectroscopy for studying the three-dimensional structures of peptides and proteins, and developing physically reliable potential energy functions for studying the conformation and molecular dynamics of biomacromolecules. The vibrational spectroscopic studies involve experimental determination of infrared and Raman spectra combined with normal mode calculations of expected vibrational frequencies. Their goal is to provide rigorous predictions of the spectra to be associated with any given structure. Since the reliability of a normal mode calculation is determined by the validity of the force field, Professor Krimm's group has worked to develop empirically refined peptide force fields, which have proven successful in analyses of the vibrational spectra of peptides, polypeptides and proteins. In an effort to develop conformation-dependent force fields, the group has turned to the refinement of better molecular mechanics energy functions, and have found a method for converting spectroscopic force fields analytically into molecular mechanics energy functions. This research involves ab initio computations, spectroscopic assignments, and development of optimum molecular mechanics functional forms.