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 AJPS  Vol.2 No.6 , December 2011
Secondary Structure Changes and Thermal Stability of Plasma Membrane Proteins of Wheat Roots in Heat Stress
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). Quantitative 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 remain 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.
Cite this paper: nullX. Zhao, Y. Shi, L. Chen, F. Sheng and H. Zhou, "Secondary Structure Changes and Thermal Stability of Plasma Membrane Proteins of Wheat Roots in Heat Stress," American Journal of Plant Sciences, Vol. 2 No. 6, 2011, pp. 816-822. doi: 10.4236/ajps.2011.26096.
References

[1]   A. S. Malik, O. Boyko, N. Atkar and W. F. Young, “A Comparative Study of MR Imaging Profile of Titanium Pedicle Screws,” Acta Radiologica, Vol. 42, No. 3, 2001, pp. 291-293. doi:10.1080/028418501127346846

[2]   Y. L. Yang, F. Zhang, W. L. He, X. M. Wang and L. X. Zhang, “Iron-Mediated Inhibition of H+-ATPase in Plasma Membrane Vesicles Isolated from Wheat Roots,” Cellular and Molecular Life Science, Vol. 60, No. 6, 2003, pp. 1249-1257.

[3]   J. L. R. Arrondo and F. M. Go?i, “Structure and Dynamics of Membrane Proteins as Studied by Infrared Spectroscopy,” Progress in Biophysics & Molecular Biology, Vol. 72, 1999, pp. 367-405.

[4]   H. Shi, L. Xiong, K. Y. Yang, C. Q. Tang, T. Y. Kuang and N. M. Zhao, “Protein Secondary Structure and Conformational Changes of Photosystem II during Heat Denaturation Studied by Fourier Transforminfrared Spectroscopy,” Journal of Molecular Structure, Vol. 446, No. 1-2, 1998, pp. 137-147.

[5]   E. Goormaghtigh, V. Raussens and J. M. Ruysschaert, “Attenuated Total Refection Infrared Spectroscopy of Proteins and Lipids in Biological Membranes,” Biochimica et Biophysica Acta, Vol. 1422, 1999, pp. 105-185.

[6]   A. M. Phelan and D. G. Lange, “Ischemia/Reperfusion -induced Changes in Membrane Fluidity Characteristics of Brain Capillary Endothelial Cells and Its Prevention by Liposomal-Incorporated Superoxide Dismutase,” Biochimica et Biophysica Acta, Vol. 1067, 1991, pp. 97-103.

[7]   R. H. Sills, D. J. Moore and R. Mendelsohn, “Erythrocyte Peroxidation: Quantitation by Fourier Transform Infrared Spectroscopy,” Analytical Biochemistry, Vol. 218, No. 1, 1994, pp. 118-123.

[8]   H. Susi, S. N. Timasheff and L. Stevens, “Infrared Spectra and Protein Conformation in Aqueous Solutions: The Amide I Band in H2O and D2O Solutions,” Jounral Biology Chemistry, Vol. 242, 1967, pp. 5460-5466.

[9]   Q. S. Qiu and X. F. Su, “The Influence of Extra Cellular Side Ca2+ on the Activity of the Plasma Membrane H+ATPase from Wheat Roots,” Australian Journal of Plant Physiology, Vol. 25, 1998, pp. 923-928.

[10]   T. Ohinish, R. S. Gall and M. L. Mayer, “An Improved Assay of Inorganic Phosphate in the Presence of Extralabile Phosphate Compounds: Application to the ATPase assay in the Presence of Phosphocreatine,” Analytical Biochemistry, Vol. 69, 1975, pp. 261-267.

[11]   M. M. Bradford, “A Rapid and Sensitive Method for the Quantization of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding,” Analytical Biochemistry. Vol. 72, 1976, pp. 248-254. doi:10.1016/0003-2697(76)90527-3

[12]   W. K. Surewicz and H. H. Mantsch, “New Insight into Protein Secondary Structure from Resolution-Enhanced Infrared Spectra,” Biochimica et Biophysica Acta., Vol. 952, No. 2, 1988, pp. 115-130. doi:10.1016/0167-4838(88)90107-0

[13]   K. Rahmelow and W. Hubner, “Infrared Spectroscopy in Aqueous Solution: Difficulties and Accuracy of Water Subtraction,” Applied Spectroscopy, Vol. 51, No. 2, 1997, pp. 160-170. doi:10.1366/0003702971940080

[14]   P. I. Haris, M. Coke and D. Chapman, “Fourier Transform Infrared Spectroscopic Investigation of Rhodopsin Structure and Its Comparison with Bacteriorhodopsin,” Biochimica et Biophysica Act, Vol. 995, No. 2, 1989, pp. 160-167. doi:10.1016/0167-4838(89)90075-7

[15]   A. Dong, P. Huang and W. S. Caughey, “Protein Seconddary Structures in Water from the Second Derivative Amide I Infrared Spectra,” Biochemistry, Vol. 29, 1990, pp. 3303-3308. doi:10.1021/bi00465a022

[16]   T. Heimburg, J. Schunemann, K. Weber and N. Geisler, “FTIR-Spectroscopy of Multistranded Coiled Coil Proteins,” Biochemistry, Vol. 38, No. 39, 1999, pp. 12727-12734. doi:10.1021/bi983079h

[17]   A. Blume, W. Hubner and G. Messner, “Fourier Transform Infrared Spectroscopy of 13C =O Laber Phospholipids Hydrogen Bonding to Carbonyl Groups,” Biochemistry, Vol. 27, No. 21, 1988, pp. 8239-8249. doi:10.1021/bi00421a038

[18]   A. Menikh and M. Fragata, “Fourier Transform Infrared Spectroscopic Study of Ion Binding and Intramolecular Interactions in the Polar Head of Digalac-tosyldiacylglycerol,” European Biophysics Journa, Vol. 22, No. 4, 1993, pp. 249-258. doi:10.1007/BF00180259

[19]   W. Z. He, W. R. Newell, P. I. Haris, D. Chapman and J. Barber, “Protein Secondary Structure of the Isolated Photosystem II Reaction Center and Conformational Changes Studied by Fourier Transform Infrared Spectroscopy,” Biochemistry, Vol. 30, No. 18, 1991, pp. 4552-4559. doi:10.1021/bi00232a027

[20]   W. K. Surewicz and H. H. Mantsch, “Infrared Absorption Methods for Examining Protein Structure,” In: H. A. Havel, Ed., Spectroscopic Methods for Determining Protein Structure in Solution, VCH, New York, 1996, pp. 135-162.

[21]   G. M. MacDonald and B. A. Barry, “Difference FT-IR Study of a Novel Biochemical Preparation of Photosystem,” Biochemistry, Vol. 31, No. 40, 1992, pp. 9848-9853. doi:10.1021/bi00155a043

 
 
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