A new method for the presentation of alignments of long sequences is described. The degree of identity for the aligned sequences is averaged for sections of a fixed number of residues. The resulting values are converted to shades of gray, with white corresponding to lack of identity and black corresponding to perfect identity. A sequence alignment is represented as a bar filled with varying shades of gray. The display is compact and allows for a fast and intuitive recognition of the distribution of regions with a high similarity. It is well suited for the presentation of alignments of long sequences, e.g. of protein superfamilies, in plenary lectures. The method is implemented as a HyperCard stack for Apple Macintosh computers. Several options for the modification of the output are available (e.g. background reduction, size of the summation window, consideration of amino acid similarity, inclusion of graphic markers to indicate specific domains). The output is a PostScript file which can be printed, imported as EPS or processed further with Adobe Illustrator.
[1]
M. Levitt.
Conformational preferences of amino acids in globular proteins.
,
1978,
Biochemistry.
[2]
S. Henikoff,et al.
Amino acid substitution matrices from protein blocks.
,
1992,
Proceedings of the National Academy of Sciences of the United States of America.
[3]
S. Morimura,et al.
Structure and function of the ftsH gene in Escherichia coli.
,
1991,
Research in microbiology.
[4]
Barry Robson,et al.
An algorithm for secondary structure determination in proteins based on sequence similarity
,
1986,
FEBS letters.
[5]
L T Hunt,et al.
The PIR protein sequence database.
,
1991,
Nucleic acids research.
[6]
A. Mclachlan.
Tests for comparing related amino-acid sequences. Cytochrome c and cytochrome c 551 .
,
1971,
Journal of molecular biology.