REFINEMENT OF PROTEIN CONFORMATIONS USING A MACROMOLECULAR ENERGY MINIMIZATION PROCEDURE

This paper presents a rapid refinement procedure capable of deriving the stable conformation of a macromolecule from experimental model co-ordinates. All the degrees of freedom of the molecule are allowed to vary and all parts of the structure are refined simultaneously in a general force-field. The procedure has been applied to myoglobin and lysozyme. The deviations of peptide bonds from planar conformation and of various bond angles from their respective average values are found to contribute significantly to the refined protein conformation. Hydrogen atoms are not included in the present refinement. A set of non-bonded potential functions, applicable to the equilibrium of a folded protein in an aqueous medium, is described and tested on myoglobin. © 1969.