Hydrophobic microdomains as structural invariant regions in proteins.
A procedure for finding clusters of interacting residues in protein hydrophobic cores is proposed. Such clusters have been located for six globular proteins of known structure. Assuming that sequences of the same protein from different biological sources encode the same tertiary structure, replacements within clusters were analysed after sequence alignment. An evolutionary conservation was found for residues in cluster positions showing that these microdomains play a structural role and are more invariant in proteins.
Płochocka
D
D
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
Zielenkiewicz
P
P
Rabczenko
A
A
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D001330:Electronic Data Processing; D006801:Humans; D009113:Muramidase; D009211:Myoglobin; D011487:Protein Conformation; D012260:Ribonucleases; D012995:Solubility
D009211:Myoglobin; D012260:Ribonucleases; D009113:Muramidase