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The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins
Author(s) -
Hiroshi Nakashima,
Ken Nishikawa
Publication year - 1992
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(92)80506-c
Subject(s) - extracellular , cytoplasm , biochemistry , transmembrane protein , cystine , intracellular , cysteine , amino acid , peptide , membrane protein , alanine , peptide sequence , threonine , chemistry , transmembrane domain , biology , membrane , serine , enzyme , receptor , gene
The amino acid composition or transmembrane proteins was analyzed for their three separate portions: the transmembrane apolar, cytoplasmic and extracellular regions. The composition was different between cytoplasmic and extracellular peptides; alanine and arginine residues were preferentially sited on the cytoplasmic side, while the threonine and cysteine/cystine were preferentially sited on the extracellular side. The composition of cytoplasmic and extracellular peptides of membrane proteins corresponded to those of intracellular and extracellular types of soluble proteins, respectively. This difference in composition was independent of the peptide orientation against the membrane. Peptide chains could be correctly assigned as either cytoplasmic or extracellular, solely from an analysis of sequence composition. For single‐spanning membrane proteins the predictive accuracy was 90%, whereas for multi‐spanning proteins this was 85%.