CROSS-SPECIES PROTEIN IDENTIFICATION USING AMINO-ACID-COMPOSITION, PEPTIDE MASS FINGERPRINTING, ISOELECTRIC POINT AND MOLECULAR-MASS - A THEORETICAL EVALUATION
Mr. Wilkins et Kl. Williams, CROSS-SPECIES PROTEIN IDENTIFICATION USING AMINO-ACID-COMPOSITION, PEPTIDE MASS FINGERPRINTING, ISOELECTRIC POINT AND MOLECULAR-MASS - A THEORETICAL EVALUATION, Journal of theoretical biology, 186(1), 1997, pp. 7-15
Proteins can be identified by rapid techniques that do not involve Edm
an degradation sequencing. These approaches entail the matching of ami
no acid compositions or tryptic peptide masses of proteins against dat
abases, often in conjunction with estimated protein molecular weight a
nd isoelectric point. As genome sequencing projects progress, proteins
from poorly molecularly defined organisms will increasingly be identi
fied by cross-species comparison to proteins from well-defined organis
ms. To investigate the application of rapid techniques for cross-speci
es protein identification, a total of 65 theoretical cross-species com
parisons involving 21 proteins (nine human and 12 E. coli) were undert
aken. The degree of conservation of amino acid composition, tryptic pe
ptides, protein isoelectric point and mass was established. Protein am
ino acid composition was well conserved across species boundaries, whi
lst tryptic peptides were poorly conserved. The molecular weight of pr
oteins was generally well conserved, but protein isoelectric point was
not. These results suggest that cross-species protein identification
by rapid techniques will be done best by protein amino acid compositio
n and protein molecular weight. (C) 1997 Academic Press Limited.