OPEN ACCESS | PEER-REVIEWED | RESEARCH ARTICLE | DOWNLOAD PDF | VIEW FULL-TEXT PDF | TOTAL VIEWS
Secondary structure investigation of bovine serum albumin (BSA) by Fourier transform infrared (FTIR) spectroscopy in the amide III region
Dongmin Li (1) , Hong Zhang (2) , Gang Ma (3,*)
(1) Key Laboratory of Medicinal Chemistry and Molecular Diagnosis of Ministry of Education, College of Chemistry and Environmental Science, Hebei University, Baoding, 071002, China
(2) Key Laboratory of Medicinal Chemistry and Molecular Diagnosis of Ministry of Education, College of Chemistry and Environmental Science, Hebei University, Baoding, 071002, China
(3) Key Laboratory of Medicinal Chemistry and Molecular Diagnosis of Ministry of Education, College of Chemistry and Environmental Science, Hebei University, Baoding, 071002, China
(*) Corresponding Author
Received: 02 Jan 2014 | Revised: 03 Feb 2014 | Accepted: 04 Feb 2014 | Published: 30 Jun 2014 | Issue Date: June 2014
Fourier transform infrared spectroscopy is widely used to analyze protein secondary structures. The common strategy in this field is to analyze the conformation sensitive 1700-1600 cm-1 amide I region of protein FTIR spectrum. Though the amide III region of protein is also sensitive to secondary structural changes, its potential for protein secondary structural analysis is largely unexplored. In this paper, we performed a detailed investigation on the second structural analysis of bovine serum albumin by monitoring the spectral variation of the amide III band under a variety of pH conditions by FTIR spectroscopy and FTIR second derivative spectroscopy. Our results show that both acidic and basic conditions have pronounced effects on the overall secondary structures of BSA, suggesting denaturation effects. Furthermore, we observe that the amide III band profiles under acidic and basic conditions appear to be quite different. Our results clearly demonstrate that the amide III region is a promising probing region for protein secondary structural analysis.
Links for Article
| | | | | | |
| | | | | | |
| | |
Article MetricsThis Abstract was viewed 1397 times | PDF Article downloaded 641 times
Natural Science Foundation of Hebei Province (No. B2011201082); Ministry of Education of China (No. 211014), China
. Xin Zhang, Zhijuan Pan
Microstructure Transitions and Dry-Wet Spinnability of Silk Fibroin Protein from Waste Silk Quilt
Polymers 11(10), 1622, 2019
. Wenjie Sun, Jia Yang, Jianzhi Zhu, Yiwei Zhou, Jingchao Li, Xiaoyue Zhu, Mingwu Shen, Guixiang Zhang, Xiangyang Shi
Immobilization of iron oxide nanoparticles within alginate nanogels for enhanced MR imaging applications
Biomaterials Science 4(10), 1422, 2016
. Byler, D. M.; Susi, H. Biopolymers 1986, 25, 469-487.
. Surewicz, W. K.; Mantsch, H. H. Biochim. Biophys. Acta 1988, 952, 115-130.
. Dong, A.; Huang, P.; Caughey, W. S. Biochemistry 1990, 29, 3303-3308.
. Goormaghtigh, E.; Cabiaux, V.; Ruysschaert, J. M. Subcell. Biochem. 1994, 23, 405-450.
. Barth, A.; Zscherp, C. Q. Rev. Biophys. 2002, 35, 369-430.
. Kong, J.; Yu, S. Acta Biochim. Biophys. Sin. 2007, 39, 549-559.
. Anderle, G.; Mendelsohn, R. Biophys. J. 1987, 52, 69-74.
. Griebenow, K.; Klibanov, A. M. Proc. Natl. Acad. Sci. U. S. A. 1995, 92, 10969-10976.
. Vedantham, G.; Sparks, H. G.; Sane, S. U.; Tzannis, S.; Przybycien, T. M. Anal. Biochem. 2000, 285, 33-49.
. Cai, S.; Singh, B. R. Biochemistry 2004, 43, 2541-2549.
. Li-Chan, E. C. Le Lait 2007, 87, 443-458.
. Estey, T.; Kang, J.; Schwendeman, S. P.; Carpenter, J. F. J. Pharm. Sci. 2006, 95, 1626-1639.
. Susi, H.; Byler, M. D. Biochem. Biophys. Res. Commun. 1983, 115, 391-397.
How to cite
The other citation formats (EndNote | Reference Manager | ProCite | BibTeX | RefWorks) for this article can be found online at: How to cite item
DOI Link: https://doi.org/10.5155/eurjchem.5.2.287-290.1007
| | | | | | | | |
| | | | | |
Save to Zotero Save to Mendeley
European Journal of Chemistry 2014, 5(2), 287-290 | doi: https://doi.org/10.5155/eurjchem.5.2.287-290.1007 | Get rights and content
- There are currently no refbacks.
© Copyright 2010 - 2021 • Atlanta Publishing House LLC • All Right Reserved.
The opinions expressed in all articles published in European Journal of Chemistry are those of the specific author(s), and do not necessarily reflect the views of Atlanta Publishing House LLC, or European Journal of Chemistry, or any of its employees.
Copyright 2010-2021 Atlanta Publishing House LLC. All rights reserved. This site is owned and operated by Atlanta Publishing House LLC whose registered office is 2850 Smith Ridge Trce Peachtree Cor GA 30071-2636, USA. Registered in USA.