Abstract: A computational method that predicts chemical and electrostatic properties of residues in proteins and utilizes information contained in those predictions to identify various interaction sites is disclosed. The various interaction sites may include, for example, cofactor binding sites, ligand binding sites, catalytic (active) sites or recognition sites. The method of the invention identifies the ionizable residues in the protein with anomalous predicted titration behavior and searches for the clustering of those residues into putative interaction sites. Practicing the method of the invention requires only the structure of the subject protein (which may be deduced, a priori, from the amino acid sequence) and, thus, may be applied to proteins that bear no similarity in structure or sequence to any previously characterized protein.

Abstract: A variable-coupling quasioptical electron paramagnetic resonance apparatus. In one embodiment, the variable-coupling quasioptical electron paramagnetic resonance apparatus includes a variable coupling quasioptical resonance cavity constructed from two back-to-back Fabry-Perot interferometers. One Fabry-Perot interferometer is formed from two partially reflecting mirrors. The second Fabry-Perot interferometer is an interferometer formed from one of the partially reflecting mirrors and a back mirror. A sample to be studied is placed within the cavity adjacent the partially reflecting mirrors and between one of the partially reflecting mirrors and the back mirror. The relative spacing of the partially reflecting mirrors and the back mirror is adjustable. With this arrangement, the interferometer can be made to act as a single mirror with variable reflectivity, thereby permitting incident radiation reaching the sample to be varied precisely and continuously.