Zobrazeno 1 - 10 of 174 pro vyhledávání: '"D Tsernoglou"'
2
The dodecameric ferritin fron Listeria innocua contains a novel intersubunit iron-binding site
Autor: A, Ilari, S, Stefanini, E, Chiancone, D, Tsernoglou
Ferritin is characterized by a highly conserved architecture that comprises 24 subunits assembled into a spherical cage with 432 symmetry. The only known exception is the dodecameric ferritin from Listeria innocua. The structure of Listeria ferritin
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::7c04b5ae6d090163e9d86038d20a7a95
http://hdl.handle.net/11573/253532
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3
The crystal structure of EcoRV endonuclease and of its complexes with cognate and non-cognate DNA fragments
Autor: F K, Winkler, D W, Banner, C, Oefner, D, Tsernoglou, R S, Brown, S P, Heathman, R K, Bryan, P D, Martin, K, Petratos, K S, Wilson
Publikováno v: The EMBO journal. 12(5)
The crystal structure of EcoRV endonuclease has been determined at 2.5 A resolution and that of its complexes with the cognate DNA decamer GGGATATCCC (recognition sequence underlined) and the non-cognate DNA octamer CGAGCTCG at 3.0 A resolution. Two
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e3291e2f229157114dc56321bd415c5a
https://pubmed.ncbi.nlm.nih.gov/8491171
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6
The Structure of Ribonuclease-S at 3.5 A Resolution
Autor: Karl D. Hardman, Tadashi Inagami, Norma M. Allewell, Frederic M. Richards, D. Tsernoglou, L.N. Johnson, Harold W. Wyckoff
Publikováno v: Journal of Biological Chemistry. 242:3984-3988
The electron density map of ribonuclease-S calculated from x-ray diffraction data on the protein and three heavy atom derivatives at 3.5 A resolution is interpretable in terms of main chain and side chain conformation with the aid of pre-existing che
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::abb0046993f07d4c34a83387946d7330
https://doi.org/10.1016/s0021-9258(18)95844-8
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8
The Three-Dimensional Structure of Ribonuclease-S
Autor: D. Tsernoglou, James R. Knox, A.W. Hanson, Benhur Lee, Harold W. Wyckoff, Frederic M. Richards
Publikováno v: Journal of Biological Chemistry. 245:305-328
The procedures used in the collection and analysis of x-ray diffraction data from single crystals of ribonuclease-S are described. Both isomorphous and anomalous scattering were measured on heavy atom derivatives prepared with the uranyl cation, the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4bedc8754efd561b10e3e55cdf0e8f22
https://doi.org/10.1016/s0021-9258(18)63395-2
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