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dc.contributor.authorTakeuchi, Yasuo
dc.contributor.authorIshikawa, Kohki
dc.contributor.authorNoguchi, Shuji
dc.contributor.authorNakamura, Kazue T.
dc.contributor.authorMizuno, Hiroshi
dc.contributor.authorMitsui, Yukio
dc.date.accessioned2023-11-03T10:50:27Z
dc.date.available2023-11-03T10:50:27Z
dc.date.issued1989
dc.date.submitted2023-11-03
dc.identifier.citationAdvances in protein design, 177 - 183en_US
dc.identifier.isbn3527280243
dc.identifier.isbn0895739534
dc.identifier.issn0930-4320
dc.identifier.urihttp://hdl.handle.net/10033/623533
dc.description.abstractThe crystal structure of Streptomyces Subtilisin Inhibitor (SSI) was partially refined by restrained least-squares methods to a conventional R value of 24 % employing rotating anode data to 1.85 A resolution range. The Sstructines of the complex of a bacterial alkaline serine proteinase, subtilisin BPN’, with its proteinaceous inhibitor SSI was partially refined to&® the (sR valuesgot 216% seupkoying lag RR synchrotron data. Comparing the B-factors between free SSI and complexed SSI, the marked rigidification of polypeptide chain segments occurred not only in the “reactive site segment” which is in direct contact with the enzyme but also in those segments which are closely connected with the reactive site segment through either covalent linkage or non-covalent interactions. Moreover the structure of the complex of subtilisin with genetically engineered mutant SSI was solved by ( F mutant - F wild ) difference Fourier syntheses.en_US
dc.language.isoenen_US
dc.publisherGBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweigen_US
dc.relation.ispartofseriesGBF monographs ; Volume 12en_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleSTRUCTURAL AND FUNCTIONAL ASPECTS OF PROTEIN-PROTEIN INTERACTION AS STUDIED THROUGH CRYSTAL STRUCTURE OF SUBTILISIN COMPLEXED WITH ITS TRAPPED SUBSTRATE SSI (STREPTOMYCES SUBTILISIN INHIBITOR)en_US
dc.typeBook chapteren_US
dc.typeconference paperen_US
dc.contributor.departmentFaculty of Pharmaceutical Sciences University of Tokyo, Hongo, Tokyo 113, Japan; National Institute of Agrobiological Resources Tsukuba, Ibaraki 305, Japan; Faculty of Engineering, Nagaoka University of Technology Nagaoka, Niigata 940-21, Japanen_US
dc.identifier.journalAdvances in protein design, 1988en_US
refterms.dateFOA2023-11-03T10:50:27Z


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