COOH-terminal decamers in proteins are non-random.
We have undertaken an exhaustive statistical analysis of the amino acid sequences at the carboxyl-terminal (C) ends of proteins. The composition of the C-terminal decapeptides differs from that expected for the given proteins from the overall amino acid composition. For E. coli, yeast, and H. sapiens it was shown that positively charged amino acid residues are over-represented while Gly residues are under-represented. The C-terminal bias, a novel feature of protein structure, should be taken into account when molecular evolution, spatial structure, translational termination and protein folding are concerned.
Berezovsky
I N
IN
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.
Kilosanidze
G T
GT
Tumanyan
V G
VG
Kisselev
L
L
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D016208:Databases, Factual; D004926:Escherichia coli; D019143:Evolution, Molecular; D005998:Glycine; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012441:Saccharomyces cerevisiae
D010446:Peptide Fragments; D011506:Proteins; D005998:Glycine