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Amino acid sequence template useful for α‐helix‐turn‐α‐helix prediction
Author(s) -
Shestopalov Boris V.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81364-4
Subject(s) - helix (gastropod) , turn (biochemistry) , alpha helix , helix turn helix , peptide sequence , sequence (biology) , polyoma virus , biology , virus , amino acid , computational biology , protein structure , microbiology and biotechnology , crystallography , chemistry , genetics , biochemistry , gene , transcription factor , dna binding protein , ecology , snail
Necessary stereochemical requirements for an amino acid sequence segment to fold into an α‐helix‐turn‐α‐helix supersecondary structure are presented in sequence template form. The usefulness of the template is illustrated by α‐helix‐turn‐α‐helix predictions consistent with experimental data from the large T antigens of two polyoma viruses, simian virus 40 (segment 143–165) and mouse polyoma virus (segment 297–319), and the yeast transcription activator GCN4 (segment 256–278).