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Title 

Expression and characterization of the integral membrane domain of bacterial histidine kinase SCO3062 for structural studies

Authors 

K J YeoSu Nam GwakH J KimC CheongMyung Hee KimY H Jeon

Publisher 

Elsevier

Issue Date 

2008

Citation 

Biochemical and Biophysical Research Communications, vol. 376, no. 2, pp. 409-413

Keywords 

hemoglobin fusionhistidine kinaseintegral membrane proteinNMRnuclear magnetic resonanceSCO3062bacterial enzymemembrane proteinprotein expressionbacterial proteins

Abstract 

Bacterial histidine kinases play an important role in the response to external stimuli. Structural studies of the histidine kinase transmembrane domain are challenging due to difficulties in protein expression and sample preparation. After carrying out expression screening of a series of histidine kinases, we investigated sample preparation methods for obtaining high quality samples of the periplasmic and transmembrane domain (PTD) of the bacterial histidine kinase SCO3062. Various sample conditions were tested for their ability to give homogeneous NMR spectra of the SCO3062 PTD with well-resolved resonances. Circular dichroism and 3D 15N-edited NOESY spectrum results demonstrate that the SCO3062 PTD is predominantly α-helical. This method should be applicable to the NMR analysis of other transmembrane proteins.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2008.09.002

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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