作者: Yekbun Adiguzel , Jörn Güldenhaupt , Carsten Kötting , Jürgen Kuhlmann , Herbert Waldmann
DOI: 10.1240/SAV_GBM_2007_M_001787
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摘要: The first high quality Amide I bands of membrane-bound Ras were obtained after establishing an ATR-FTIR set-up. Protein secondary structure analyses performed by improved curve-fitting technique. Truncated H-Ras (1-166) and N-Ras (1-188) protein structures in accordance with the literature. Tyr side chain band splitting was observed for N-Ras. Besides, deviations apparent, when there no membrane available to binding. Measurements also polarized light. The study interaction nitric oxide initiated a model system. activity attained. lipid absorption intensity modulated. In relation, random sheet transitions observed. Stabilizing interactions C=O region accompanying. This could be associated conformational changes protein.