Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Evangelos Papamokos"'
Autor:
Evangelos Papamokos, Giuseppina Gatti, E Menagatti, Martino Bolognesi, Mario Guarneri, Robert Huber, Markus Marquart
Publikováno v:
Journal of Molecular Biology. 162:839-868
The three-dimensional structure of the proteic complex formed by bovine trypsinogen and the porcine pancreatic secretory trypsin inhibitor (Kazal type) has been solved by means of Patterson search techniques, using a predicted model of the trypsin-ov
Autor:
Mark W. Empie, Evangelos Papamokos, I. Kato, Ernst Weber, Robert Huber, Wolfram Bode, M. Laskowski
Publikováno v:
Journal of Molecular Biology. 158:515-537
Japanese quail ovomucoid third domain (OMJPQ3), a Kazal-type inhibitor, was crystallographically refined with energy constraints. The final R-value is 0.20 at 1.9 A resolution. The four molecules in the asymmetric unit are very similar, with deviatio
Publikováno v:
European Journal of Biochemistry. 166:673-692
Triclinic crystals of the complex formed by eglin with subtilisin Carlsberg were analyzed by X-ray diffraction. The crystal and molecular structure of this complex was determined with data that extended to 0.12-nm resolution by a combination of Patte
Autor:
W. C. Bogard, Ernst Weber, Mark W. Empie, Evangelos Papamokos, Wolfram Bode, I. Kato, Robert Huber, William J. Kohr, Wojciech Ardelt, Michael Laskowski
Publikováno v:
Structural and Functional Aspects of Enzyme Catalysis ISBN: 9783642817403
Beyond the purely descriptive phases, long-term biochemical investigations may have algorithmic or mechanistic objectives. The ultimate hope of the algorithmic approach is the elucidation of the organismic characteristics from the nucleotide sequence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9b1e0f83f337c489076165d2d8d499e3
https://doi.org/10.1007/978-3-642-81738-0_13
https://doi.org/10.1007/978-3-642-81738-0_13
Publikováno v:
Journal of molecular biology. 149(1)
The third domain of Japanese quail ovomucoid, a Kazal type inhibitor, has been crystallized and its crystal structure determined at 2.5 A resolution using multiple isomorphous replacement techniques. The asymmetric unit contains four molecules. In th
Publikováno v:
European Journal of Biochemistry. 8/3/87, Vol. 166 Issue 3, p673-692. 20p. 15 Diagrams, 10 Charts, 4 Graphs.