Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases
- 6 January 1986
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 194 (2) , 338-346
- https://doi.org/10.1016/0014-5793(86)80113-2
Abstract
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.Keywords
This publication has 20 references indexed in Scilit:
- Mammalian ribonucleasesFEBS Letters, 1985
- Rat pancreatic ribonuclease: agreement between the corrected amino acid sequence and the sequence derived from its messenger RNAFEBS Letters, 1983
- Ribonuclease-A: least-squares refinement of the structure at 1.45 Å resolutionActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1982
- The Amino‐Acid Sequence of Kangaroo Pancreatic RibonucleaseEuropean Journal of Biochemistry, 1978
- The molecular evolution of pancreatic ribonucleaseJournal of Molecular Evolution, 1977
- Invariant features of the structure of pancreatic ribonucleaseJournal of Molecular Biology, 1977
- Relationship between α-helical propensity and formation of the ribonuclease-S complexJournal of Molecular Biology, 1975
- Algorithms for prediction of α-helical and β-structural regions in globular proteinsJournal of Molecular Biology, 1974
- Prediction of protein conformationBiochemistry, 1974
- Biological Function of Pancreatic RibonucleaseNature, 1969