Proteins are functional molecules that maintain and manage life. Their functions emerge at their folding state and their unique structures in this state are determined only from their sequences. The interconnection of DNA sequence-protein-fold-function-life forms, is often represented by an aspect of life that consists of one-dimensional sequences (protein sequences and DNA), but we have not yet elucidated the whole mechanism of the transformation from sequence to life. One step in elucidating the mechanism is the prediction of protein structures from amino-acid sequences. Recently, an effective method (structure (3D)-sequence (1D) compatibility evaluation) was developed using the database of protein structures and sequences. A number of successful predictions show the validity of this method.

Subjects investigated in our laboratory are as follows:

• Structure prediction of structure-unknown proteins using the 3D-1D compatibility evaluation (forward-folding search)
• Development of methodology of the 3D-1D compatibility evaluation
• Search of sequences compatible with a probe structure against the sequence database (inverse-folding search)
• Structure stability analysis of mutant proteins using a 3D-profile
• Secondary structure prediction based on the 3D-1D compatibility evaluation
• Development of novel methods to predict protein structures from sequences
• Analyses of genomes
• Development of a protein mutant database (PMD)