Coherent two-dimensional infrared spectroscopy: Quantitative analysis of protein secondary structure in solution
Name
Protein_2DIR_Spectra.zip
Description
Experimental FTIR and 2D IR Spectra
Size
2.03 MB
Format
ZIP
Checksum (MD5)
eaa5b523368864cd7a63ba086bedede7
Author(s)
Tokmakoff, Andrei
Jones, Kevin C.
Reppert, Mike E.
Peng, Chunte Sam
Baiz, Carlos R.
Date Issued
March 1, 2012
Publisher
Royal Society of Chemistry
Citation
Baiz, Carlos R. et al. “Coherent Two-dimensional Infrared Spectroscopy: Quantitative Analysis of Protein Secondary Structure in Solution.” The Analyst 137.8 (2012): 1793
Abstract
We present a method to quantitatively determine the secondary structure composition of globular proteins using coherent two-dimensional infrared (2DIR) spectroscopy of backbone amide I vibrations (1550–1720 cm−1). Sixteen proteins with known crystal structures were used to construct a library of 2DIR spectra, and the fraction of residues in α-helix, β-sheet, and unassigned conformations was determined by singular value decomposition (SVD) of the measured two-dimensional spectra. The method was benchmarked by removing each individual protein from the set and comparing the composition extracted from 2DIR against the composition determined from the crystal structures. To highlight the increased structural content extracted from 2DIR spectra a similar analysis was also carried out using conventional infrared absorption of the proteins in the library.
Subjects
spectroscopy, ultrafast, two-dimensional infrared, protein structure
Terms of Use
Attribution-NonCommercial-ShareAlike 3.0 United States
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