Study of protein folding hierarchy by two-dimensional infrared technique (2D-IR)

• Grant number: 07/03574-7
• Support Opportunities: Scholarships in Brazil - Scientific Initiation
• Start date: May 01, 2008
• End date: December 31, 2009
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Principal Investigator: Marinônio Lopes Cornélio
• Grantee: Patricia Suemy Kumagai
• Host Institution: Instituto de Biociências, Letras e Ciências Exatas (IBILCE). Universidade Estadual Paulista (UNESP). Campus de São José do Rio Preto. São José do Rio Preto , SP, Brazil

Abstract

From the use of Infrared technique with Transformed of Fourier and Two-dimensional Correlation (2D-IR) Applied to the Proteins, is possible to determine minimal conformacional changes and if mainly exists some correlation between vibracional modes that are utilized for designate the different components of the secondary structure in proteins and peptídeos. The conformacional changing is prompted by external stimuli such as, temperature, pH and pressure. The deconvolution analysis by Fourier (FSD) or spectrum difference are shown limited for establish such correlation. So the application of 2D-IR in the inquiry on the process of protein folding/unfolding, as well as the dimerization of monomers can obtain new information of the sequential evolution of the folding/unfolding of a protein, and monitor the contacts inter and intra protein.