Zobrazeno 1 - 10
of 40
pro vyhledávání: '"J. J. Stezowski"'
Autor:
J. J. Stezowski, E. Eckle
Publikováno v:
Steric Aspects of Biomolecular Interactions ISBN: 9781351076890
Steric Aspects of Biomolecular Interactions
Steric Aspects of Biomolecular Interactions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5e6b18c301eb13a9b61fdac4f7f89ecd
https://doi.org/10.1201/9781351076890-5
https://doi.org/10.1201/9781351076890-5
Autor:
Jeffrey R.D. DeBord, M. C. Davies, Robert C. Tisdale, J. J. Stezowski, C. R. Ross, T. A. George, K. Heier, E. J. Haas
Publikováno v:
Acta Crystallographica Section C Crystal Structure Communications. 53:1251-1254
The crystal structure of [bis(2-diphenylphosphinoethyl)phenylphosphine-P,P',P][bis(diphenylphosphino)-methane-P,P'] carbonylmolybdenum(0), [Mo(dpepp)-(dppm)(CO)] [where dppm = Ph 2 PCH 2 PPh 2 and dpepp = Ph 2 PCH 2 CH 2 P(Ph)CH 2 CH 2 PPh 2 ], is re
Publikováno v:
ChemInform. 23
Publikováno v:
ChemInform. 30
Autor:
W. L. Duax, Ž. Ružić-Toroš, Biljana Nigović, D. Horvatić, N. Bresciani-Pahor, J. J. Stezowski, Volker Magnus, Biserka Kojić-Prodić
Publikováno v:
Acta Crystallographica Section B Structural Science. 47:107-115
The crystal structures of six biologically active cnojugates of the plant growth hormone (auxin), indole-3-acetic acid (IAA), with the amino acids L-alanine (1), alpha-amino-L-butyric acid (2), L-norvaline (3), DL-aspartic acid (4), L-isoleucine (5),
Publikováno v:
Acta Crystallographica Section C Crystal Structure Communications. 53:45-47
The structure of tricarbonyl[(1,2,3,4,5-η)-2-methoxy-2,4-cyclohexadien-1-yl]iron(1+) tetrafluoroborate, [Fe(C7H9O)(CO)3]BF4, is reported. Although the tetrafluoroborate salt crystallizes in a different space group to the previously reported hexafluo
Publikováno v:
Journal of the American Chemical Society. 123(40)
Cyclodextrins (CDs) are cyclic oligosaccharides that encapsulate various small organic molecules, forming inclusion complexes. Because CD complexes are held together purely by noncovalent interactions, they function as excellent models for the study
Publikováno v:
Journal of molecular biology. 297(4)
The homodimeric enzyme form of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa ATCC 17933 crystallizes readily with the space group R3. The X-ray structure was solved at 2.6 A resolution by molecular replacement. Aside from differences
Autor:
W, Parker, J J, Stezowski
Publikováno v:
Proteins. 25(2)
A major bottleneck in the field of biochemistry is our limited understanding of the processes by which a protein folds into its native conformation. Much of the work on this issue has focused on the conserved core of the folded protein. However, one
Autor:
J. J. Stezowski, K. H. Jogun
Publikováno v:
Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 35:2306-2310