Detail of "51908-46-4"

Reference

6-N-dimethylaminonaphthylsulfonylaziridine

6-N-dimethylaminonaphthylsulfonylaziridine. Bolognesi, M.; Rossi, G. (Ist. Cristallogr. 51908-46-4 are also occured in this study., Univ. Pavia, Pavia, Italy). Acta Crystallogr., Sect. B, B33(1), 122-4 (English) 1977. CODEN: ACBCAR. DOCUMENT TYPE: Journal CA Section: 75 (Crystallization and Crystal Structure) Section cross-reference(s): 27, 26 The title compd. is monoclinic, space group P21/a, with a 22.277(2), b 7.469(2), c 8.001(1) .ANG., and .beta. 100.18(8).degree.; Z = 4; final R = 0.040 for 1233 intensities with I > .sigma.(I). The naphthalene system is not planar; the sulfone-group tetrahedron is very distorted with evidence of interaction between S dxy and C pp orbitals. The aziridine group shows the angles, but not bond lengths, expected from other measurements of systems contg. this group. The N-dimethylamino group has the usual geometry. .

Human rhinovirus capsid dynamics is controlled by canyon flexibility

Human rhinovirus capsid dynamics is controlled by canyon flexibility. Reisdorph, Nichole; Thomas, John J.; Katpally, Umesh; Chase, Elaine; Harris, Ken; Siuzdak, Gary; Smith, Thomas J. (The Scripps Center for Mass Spectrometry and the Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA). Virology, 314(1), 34-44 (English) 2003 Elsevier Science. CODEN: VIRLAX. ISSN: 0042-6822. DOCUMENT TYPE: Journal CA Section: 10 (Microbial, Algal, and Fungal Biochemistry) Section cross-reference(s): 1 Quant.Several reagents with their cas registry numbers 153168-05-9 and 51908-46-4 are used here. enzyme accessibility expts. using nano liq. chromatog. electrospray mass spectrometry combined with limited proteolysis and isotope-labeling was used to examine the dynamic nature of the human rhinovirus (HRV) capsid in the presence of three antiviral compds., a neutralizing Fab, and drug binding cavity mutations. Using these methods, it was found that the antivirals WIN 52084 and picovir (pleconaril) stabilized the capsid, while dansylaziridine caused destabilization. Site-directed mutations in the drug-binding cavity were found to stabilize the HRV14 capsid against proteolytic digestion in a manner similar to WIN 52084 and pleconaril. Antibodies that bind to the NIm-IA antigenic site and penetrate the canyon were also obsd. to protect the virion against proteolytic cleavage. These results demonstrate that quantifying the effects of antiviral ligands on protein "breathing" can be used to compare their mode of action and efficacy. In this case, it is apparent that hydrophobic antiviral agents, antibodies, or mutations in the canyon region block viral breathing. Therefore, these studies demonstrate that mobility in the canyon region is a major determinant in capsid breathing. .