Sequential unfolding events in proteins monitored by 2D correlation analysis of FTIR spectra

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DOIResolve DOI: http://doi.org/10.1063/1.1302852
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TypeBook Chapter
Proceedings titleTwo-Dimensional Correlation Spectroscopy
Series titleAIP Conference Proceedings; Volume 503
ConferenceTwo-Dimensional Correlation Spectroscopy, August 29-September 1, 1999, Kobe-Sanda, Japan
ISSN0094-243X
1551-7616
ISBN1563969165
Pages95102; # of pages: 8
AbstractThe Cro-V55C (cysteine cross-linked) dimer of the λ Cro repressor protein undergoes thermal unfolding in two discrete steps. The secondary structure of the stable equilibrium intermediate exhibits partial unfolding and reorganization at the N-terminal ends while other parts of the structure (some of the β-sheets) remain intact. To test whether the transition from the native to the intermediate state involves sequential events, we used a 2D-IR approach capable of detecting small differences of individual spectral features in response to external factors. The 2D-IR analysis shows that the intermediate state is formed in closely related sequential steps. To interpret the experimental 2D-IR data, 2D correlation plots for single and multiple sequential events were simulated. These plots were compared with the experimental data and translated into structural changes occurring within Cro-V55C. They reveal that the formation of the stable intermediate starts with the unfolding of the short N-terminal β-strand, followed by that of the three α-helices, and ends with the rearrangement of the remaining major β-sheet.
Publication date
PublisherAmerican Institute of Physics
AffiliationNRC Institute for Biodiagnostics; National Research Council Canada
Peer reviewedYes
NRC number1818
NPARC number9147528
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Record identifier58316ad6-aed1-4459-9fca-6df2327f9782
Record created2009-06-25
Record modified2016-10-04
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