Organization of diphtheria toxin T domain in bilayers: A site-directed spin labeling study

Science

Volumn 273, Issue 5276, 1996, Pages 810-812

  Oh, Kyoung Joon ^a   Zhan, Hangjun ^a   Cui, Can ^a   Hideg, Kálmán ^a   Collier, R John ^a   Hubbell, Wayne L ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

DIPHTHERIA TOXIN; NITROXIDE; WATER;

ALPHA HELIX; ARTICLE; BILAYER MEMBRANE; HYDROPHOBICITY; MEMBRANE CHANNEL; PRIORITY JOURNAL; PROTEIN DOMAIN; SPIN LABELING; TOXIN STRUCTURE;

EID: 0001350946     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5276.810     Document Type: Article

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38. 2-terminus.
39. 2 concentration was that in equilibrium with air, and the concentration of NiEDDA was 200 mM.
40. Supported by NIH grants AI-22021 and AI-22848 (R.J.C.) and EY-05216 (W.L.H.), Hungarian National Research Foundation grant OTKA/T017842 (K.H.), and the Jules Stein Professor Endowment (W.L.H.). We thank M. J. Bennett, C. E. Bell, and D. Eisenberg for providing the coordinates of the refined DT crystal structure, and D. Eisenberg, J. R. Trudell, D. Bok, C. Altenbach, H. Mchaourab, D. Farrens, and R. Langen for reading the manuscript and helpful discussions.