期刊
COLLOIDS AND SURFACES B-BIOINTERFACES
卷 25, 期 4, 页码 335-346出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0927-7765(01)00331-9
关键词
Arg-Cys; Arg-cysteamine; arginine; G-proteins; infrared reflection absorption spectroscopy; surface plasmon resonance; X-ray photoelectron spectroscopy
The dipeptide, Arg-Cys, and the related molecule, Arg-cysteamine, are adsorbed to gold surfaces and the monolayers are characterized. Chemical binding and electronic structure of the monolayers are obtained by X-ray photoelectron spectroscopy (XPS). Strong molecular binding of the adsorbates to gold surface through the sulfur atom is attained. Orientation of the adsorbates on gold is studied using infrared reflection absorption spectroscopy (IRAS). Arg-Cys is interpreted to be adsorbed on gold in a compact configuration. The Arg-cysteamine molecule is adsorbed on gold with the main molecular axis perpendicular to the surface. Interaction of G-protein with the adsorbates was studied using the surface plasmon resonance (SPR) technique. It is believed that arginine has a major role in G-protein recognition since the G-protein-coupled receptor (GPCR) alpha(2)A has an arginine-rich region in the G-protein-binding part of the third intracellular loop. (C) 2002 Elsevier Science B.V. All rights reserved.
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