Two-dimensional cross correlation analysis of protein unfolding : portrayal of the thermal denaturation of CMP kinases in the absence and presence of substrates

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DOIResolve DOI: http://doi.org/10.1063/1.1302851
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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
Pages8594; # of pages: 10
SubjectEnzymes; Nucleotides; Proteins; Infrared spectra; Secondary structure
AbstractThe functional role of CMP kinases is to regenerate mono-phosphate nucleotides in cells by transferring phosphate residues from tri-phosphorylated nucleotides to monophosphorylated nucleotides. These enzymes possess two binding sites and maintain a highly conserved secondary structure. They are essential for cell survival. Herein we compare the infrared spectra of two similar, but not identical enzymes, the CMP kinases from Escherichia coli and Bacillus subtilis. A two-dimensional cross correlation analysis of the infrared spectra reveals differences in the denaturation behavior of the two proteins. Different secondary structure elements show different time-delayed or advanced unfolding events in the two enzymes. When bound to the active sites, the two nucleotide-substrates CMP and ATP exert a stabilizing effect on the structure of both proteins. The changes observed upon thermal denaturation are different for the two enzymes. Model 2D correlations are used to simulate the different denaturation of the two enzymes. Thermal denaturation and aggregation can be distinguished as two processes separated in time.
Publication date
PublisherAmerican Institute of Physics
AffiliationNRC Institute for Biodiagnostics; National Research Council Canada
Peer reviewedYes
NRC number1822
NPARC number9148476
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Record identifier4cda896d-3d2b-4048-9be5-d05bdf355a8e
Record created2009-06-25
Record modified2016-10-07
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