secondary structure changes and thermal stability of plasma membrane proteins of wheat roots in heat stress二级结构的变化和热稳定性小麦根系质膜蛋白质的热应力.pdf

American Journal of Plant Sciences , 2011, 2, 816-822 doi:10.4236/ajps.2011.26096 Published Online December 2011 (http://www.SciRP.org/journal/ajps) Secondary Structure Changes and Thermal Stability of Plasma Membrane Proteins of Wheat Roots in Heat Stress 1 1 2 3 1 Xin Zhao , Yong Shi , Li Chen , Fenlin Sheng , Haiyan Zhou 1Laboratory of Plant Stress Ecophysiology and Biotechnology, Cold and Arid Regions Environmental and Engineering Research Institute, Chinese Academy of Sciences, Lanzhou, China; 2College of Life Science and Engineering, The Northwest University for Nationalities, Lanzhou, China; 3Instrumental Analysis and Research Center, Lanzhou University, Lanzhou, China. Email: zhaox@ Received July 21st, 2011; revised August 20th, 2011; accepted September 6th, 2011. ABSTRACT The wheat roots membrane separates the cell from the environment around it and encloses the cell contents. The pro- tein secondary structure and thermal stability of the plasma membrane of wheat root have been characterized in D2O buffer from 20 ˚C to 90 ˚C by Attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR). Quantita- tive analysis of the amide I band (1700 - 1600 cm–1) showed that the plasma membrane proteins contains 41% α-helix, 16% β-sheet, 18% turn, and 25% disorder structures at 20 ˚C. At elevated temperatures from 25 ˚C up to 90 ˚C, the α-helix and the β-sheet structure unfold into turns and the disorder structure, with a major conformational transition occurring at 50 ˚C. There is a rapid decline in H+-ATPase activity of plasma membrane from 35 ˚C to 55 ˚C and it re- main very low level H+-ATPase activity of PM from 55 ˚C to 90 ˚C. Therefore the protein conformational transition was one of reasons of loses H+-ATPase activity of plasma membrane. Keywords : Plasma Membrane, Heat Stress, Protein Second Stru