Zobrazeno 1 - 10
of 219
pro vyhledávání: '"F.A. Quiocho"'
Publikováno v:
Nature Structural Biology. 9:764-770
The first X-ray structures of an intein-DNA complex, that of the two-domain homing endonuclease PI-SceI bound to its 36-base pair DNA substrate, have been determined in the presence and absence of Ca(2+). The DNA shows an asymmetric bending pattern,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd3ad4ae51a475dc43de89bb46b0b954
https://doi.org/10.1038/nsb840
https://doi.org/10.1038/nsb840
Publikováno v:
Journal of Biological Chemistry. 266:21375-21380
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::175e387e62e4cbbebf8dae6f6e49e4fb
https://doi.org/10.1016/s0021-9258(18)54647-0
https://doi.org/10.1016/s0021-9258(18)54647-0
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 52:C242-C242
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2f356b5b474357990f974366834fe9ee
https://doi.org/10.1107/s0108767396089726
https://doi.org/10.1107/s0108767396089726
Autor:
F.A. Quiocho
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 49:c94-c94
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3288b02bd6ba7150ce7899240432b9a9
https://doi.org/10.1107/s0108767378097305
https://doi.org/10.1107/s0108767378097305
Autor:
J.W. Pflugrath, F.A. Quiocho
Publikováno v:
Journal of Biological Chemistry. 255:6559-6561
The structure of D-galactose-binding protein, a receptor for both high affinity active transport system and chemotaxis in Escherichia coli, has been solved at 4.1 A resolution using three heavy atom derivatives. The molecule is ellipsoidal with dimen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9cce44c9615fa87a29d165fed3a0a4cb
https://doi.org/10.1016/s0021-9258(18)43604-6
https://doi.org/10.1016/s0021-9258(18)43604-6
Publikováno v:
Journal of Biological Chemistry. 257:1131-1133
Theoretical conformational energy calculations show that large changes in the width of the binding-site cleft in the L-arabinose-binding protein involve only modest changes in the protein internal energy. Solvation energy changes associated with such
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::031c043396c71e25b5652bf3e5e9d6af
https://doi.org/10.1016/s0021-9258(19)68161-5
https://doi.org/10.1016/s0021-9258(19)68161-5
Autor:
F.A. Quiocho
Publisher Summary This chapter describes the technique of immobilizing single protein crystals, presents data on the properties of such crystals, and discusses the uses of insolubilized protein crystals in X-ray diffraction analysis and in studies of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7c9e0c40184f677fa293559cf8f480a7
https://doi.org/10.1016/s0076-6879(76)44040-5
https://doi.org/10.1016/s0076-6879(76)44040-5
Publikováno v:
Journal of Molecular Graphics. 1:53-54
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3317625f49946b257f54188dbadaebfc
https://doi.org/10.1016/0263-7855(83)80020-4
https://doi.org/10.1016/0263-7855(83)80020-4
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