MASIA searches for consistent patterns in multiple aligned
sequences. Predictions of secondary structures and inside/outside properties of
residues at each position in an aligned sequences are based on generalized rules for
globular proteins, which are derived from observations of known 3D-structure of
proteins. The secondary and tertiary structure of a protein is related to chemical
characterisitics of the individual amino acid residues, but a clear picture of the
secondary structure may not be apparent for one protein sequence alone. Comparing
many aligned, related sequences can reveal patterns of sequence conservation
that indicate the location of residues essential for the function, folding or
solubility of the protein. The rules are manipulated as
macros (i.e., corresponding
combinations of commands) to predict
specific properties. Before using MASIA, the best possible alignment of the
protein with other proteins in the SWISS-PROT database should be obtained.
MASIA uses as input files generated with PileUp or ClustalW. The simplified
applications can be directly accessed through this form. An on-line manual
is available. Comments are welcome, please mail them to Werner Braun.