caa a22 4500 475845560 CHVBK 20180406123913.0 cr unu---uuuuu 170329e20000801xx s 000 0 eng 10.1007/PL00000767 doi (NATIONALLICENCE)springer-10.1007/PL00000767 Localization and analysis of nonpolar regions in onconase [Elektronische Daten] [E. Y. Kolbanovskaya, A. C. Terwisscha van Scheltinga, V. G. Mukhortov, W. Ardelt, J. J. Beintema*, M. Y. Karpeisky**] Abstract.: A detailed analysis of the composition and properties of hydrophobic nuclei and microclusters has been carried out for onconase. Two main hydrophobic nuclei in the onconase structure were detected. Their composition and shape were found to be very similar to those of RNase A, in accordance with the predictions made. The nuclei in onconase are more compact, the side-chain atoms of residues included in the nuclei in onconase form more contacts with the environment than in RNase A. The hydrophobic nuclei should be considered as individual structural units along with elements of the secondary structure. Differences in composition and conformation of exposed loops between onconase and RNase A were found. The additional hydrophobic clusters attached to the nuclei in onconase might be involved in the fixation of an appropriate conformation of site(s) for manifestation of the biological activity of onconase. A comparison of amphibian representatives of the RNase A superfamily was also made. The results obtained suggest that the availability of nonpolar residues in established key positions of amino acid sequences determines the characteristic fold of homologous proteins and the structure of the active site cleft. Birkhäuser Verlag Basel,, 2000 Key words. Amphibians nationallicence hydrophobic nuclei nationallicence nonpolar contacts nationallicence onconase nationallicence ribonuclease A superfamily nationallicence Kolbanovskaya E. Y. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 117984 (Russia), RU aut Terwisscha van Scheltinga A. C. Departments of Biochemistry and Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen (The Netherlands), Fax +31 50 3634165, e-mail: beintema@chem.rug.nl, NL aut Mukhortov V. G. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 117984 (Russia), RU aut Ardelt W. Alfacell Corporation, Bloomfield (New Jersey 07003, USA), US aut Beintema* J. J. Departments of Biochemistry and Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen (The Netherlands), Fax +31 50 3634165, e-mail: beintema@chem.rug.nl, NL aut Karpeisky** M. Y. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 117984 (Russia), RU aut https://doi.org/10.1007/PL00000767 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/PL00000767 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kolbanovskaya E. Y. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 117984 (Russia), RU aut NATIONALLICENCE 700 1- Terwisscha van Scheltinga A. C. Departments of Biochemistry and Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen (The Netherlands), Fax +31 50 3634165, e-mail: beintema@chem.rug.nl, NL aut NATIONALLICENCE 700 1- Mukhortov V. G. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 117984 (Russia), RU aut NATIONALLICENCE 700 1- Ardelt W. Alfacell Corporation, Bloomfield (New Jersey 07003, USA), US aut NATIONALLICENCE 700 1- Beintema* J. J. Departments of Biochemistry and Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen (The Netherlands), Fax +31 50 3634165, e-mail: beintema@chem.rug.nl, NL aut NATIONALLICENCE 700 1- Karpeisky** M. Y. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, Moscow 117984 (Russia), RU aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer