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Amino acid sequence alignment of cereal storage proteins
Author(s) -
Reeck Gerald R.,
Hedgcoth Charles
Publication year - 1985
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(85)81088-7
Subject(s) - glutenin , hordein , storage protein , sequence (biology) , peptide sequence , amino acid , biology , computational biology , similarity (geometry) , biochemistry , chemistry , genetics , computer science , artificial intelligence , gene , protein subunit , image (mathematics)
An alignment is presented of portions of the amino acid sequences of two gliadins and a glutenin from wheat and of a barley hordein. The two gliadins exhibit similarity over much of their sequences. The glutenin is similar in sequence to the gliadins only over a restricted region. Our analysis of the aligned sequences leads us to suggest the word ‘modular’ to describe the architecture of these proteins. The term is intended to connote the joining together, in the course of evolution, of several units (modules) of distinctive character, under a set of rules that allows considerable flexibility in the arrangement of modules within a molecule.