The main research interest of the Section is to use and develop theoretical means to study the forces that govern the structure and interaction of globular protein molecules, to predict the three- dimensional structure of these molecules, and to engineer protein molecules with improved properties. Following were accomplished: (1) The laboratory's general-purpose, graphics-oriented programs, GEMM, GPLOT, and SPLOT, have been updated and improved. (2) Proved, by means of simple computer simulations of pure liquids, that the hydrophobicity does not arise from the hydrogen bonding property of water. (3) Devised a theoretical scheme by which the change in stability of a protein molecule upon point mutation can be understood and estimated from the small molecule data on hydrophobicities. (4) A method was devised that identifies possible folding initiation sites of a protein molecule when only its sequence information is given and a method is being developed to predict the three-dimensional structure of these initiation sites. (5) Structural pattern recognition analysis was made on the alpha/beta barrel motif of the protein structure. All known protein structures that have this motif can be automatically aligned using these recognized patterns. These patterns will be used in the future to spot the alpha/beta barrel structural motif from the sequence of unknown proteins. (6) A pair of potential interchain disulfide bonding sites in the Fv fragment of the immunoglobulins was identified. These bonds are expected to stabilize the Fv fragment. These sites can be located for any immunoglobulin from the sequence alignment alone.