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Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases
Author(s) -
Beintema Jaap J.,
van der Laan Jan M.
Publication year - 1986
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(86)80113-2
Subject(s) - chelydra , ribonuclease , turtle (robot) , residue (chemistry) , pancreatic ribonuclease , chemistry , bovine pancreatic ribonuclease , biochemistry , invariant (physics) , amino acid , amino acid residue , biology , stereochemistry , peptide sequence , ecology , mathematics , rna , gene , mathematical physics
There are 33 invariant amino acid positions out of 132 positions in 42 investigated sequences of ribonucleases from a number of mammalian species and a reptile (snapping turtle, Chelydra serpentina ). These invariant residues are unequally distributed over 3 different parts of the molecule. The lobe of the S‐protein part of the molecule, which lacks one disulfide bridge and has two shortened loops in turtle ribonuclease, has the lowest percentage of invariant residues, although the active‐site residue His 119 is located in this part.