Why Us? >>

  • - Open Access
  • - Peer-reviewed
  • - Rapid publication
  • - Lifetime hosting
  • - Free indexing service
  • - Free promotion service
  • - More citations
  • - Search engine friendly

Free SCIRP Newsletters>>

Add your e-mail address to receive free newsletters from SCIRP.

 

Contact Us >>

WhatsApp  +86 18163351462(WhatsApp)
   
Paper Publishing WeChat
Book Publishing WeChat
(or Email:book@scirp.org)

Article citations

More>>

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.

has been cited by the following article:

  • TITLE: Secondary Structure Changes and Thermal Stability of Plasma Membrane Proteins of Wheat Roots in Heat Stress

    AUTHORS: Xin Zhao, Yong Shi, Li Chen, Fenlin Sheng, Haiyan Zhou

    KEYWORDS: Plasma Membrane, Heat Stress, Protein Second Structure, ATR-FTIR

    JOURNAL NAME: American Journal of Plant Sciences, Vol.2 No.6, December 30, 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). 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.