| DOI | Resolve DOI: https://doi.org/10.1063/1.1302852 |
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| Author | Search for: Fabian, Heinz; Search for: Mantsch, Henry H.1; Search for: Schultz, Christian P. |
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| Affiliation | - National Research Council Canada. NRC Institute for Biodiagnostics
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| Format | Text, Book Chapter |
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| Conference | Two-Dimensional Correlation Spectroscopy, August 29 - September 1, 1999, Kobe-Sanda, Japan |
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| Abstract | The 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. |
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| Publication date | 2000-03-10 |
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| Publisher | American Institute of Physics |
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| Series | |
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| Peer reviewed | Yes |
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| NRC number | NRC-IBD-1818 |
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| NPARC number | 9147528 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 58316ad6-aed1-4459-9fca-6df2327f9782 |
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| Record created | 2009-06-25 |
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| Record modified | 2020-06-12 |
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