NDLI: Adsorption of protein GlnB of Herbaspirillum seropedicae on Si(111) investigated by AFM and XPS

Content Provider	Springer Nature Link
Author	Lubambo, A. F. Benelli, E. M. Klein, J. Schreiner, W. Camargo, P. C.
Copyright Year	2006
Abstract	The protein GlnB-Hs (GlnB of Herbaspirillum seropedicae) in diazotroph micro-organisms signalizes levels of nitrogen, carbon, and energy for a series of proteins involved in the regulation of expression and control of the activity of nitrogenase complex that converts atmospheric nitrogen in ammonia, resulting in biological nitrogen fixation. Its structure has already been determined by X-ray diffraction, revealing a trimer of (36 kDa) with lateral cavities having hydrophilic boundaries. The interactions of GlnB-Hs with the well-known Si(111) surface were investigated for different incubation times, protein concentrations in initial solution, deposition conditions, and substrate initial state. The protein solution was deposited on Si(111) and dried under controlled conditions. An atomic force microscope operating in dynamic mode shows images of circular, linear, and more complex donut-shaped protein arrangement, and also filament types of organization, which vary from a few nanometers to micrometers. Apparently, the filament formation was favored because of protein surface polarity when in contact with the silicon surface, following some specific orientation. The spin-coating technique was successfully used to obtain more uniform surface covering.
Starting Page	503
Ending Page	511
Page Count	9
File Format	PDF
ISSN	10859195
Journal	Cell Biochemistry and Biophysics
Volume Number	44
Issue Number	3
e-ISSN	15590283
Language	English
Publisher	Humana Press
Publisher Date	2006-01-01
Publisher Place	Totowa
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biochemistry Pharmacology/Toxicology Biotechnology Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Biochemistry Biophysics

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