Two-dimensional IR correlation spectroscopy: Sequential events in the unfolding process of the λ Cro-V55C repressor protein

Fabian, Heinz; Mantsch, Henry H.; Schultz, Christian

doi:10.1073/pnas.96.23.13153

Cited by 77 publications

(67 citation statements)

References 20 publications

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“…Temperature-induced change of IR spectra for protein unfolding process was reported by Fabian et al [52]. Not fully cooperative sequential unfolding of l Cro-V55C repressor protein of bacteriophage l was detected.…”

Section: Proteins and Other Biomoleculesmentioning

confidence: 82%

“…The combination of Fourier self-deconvolution and 2D correlation analysis is getting especially popular among those analyzing vibrational spectra of biological samples [52][53][54][55][56]. The motivation here is to take the full advantage of high-resolution feature of 2D spectra by combining with Fourier self-deconvolution to enhance the band discrimination.…”

Section: Pre-treatment and Post-treatment Of Datamentioning

confidence: 98%

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Advances in two-dimensional correlation spectroscopy

Noda

2004

Vibrational Spectroscopy

235

149

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Section: Proteins and Other Biomoleculesmentioning

confidence: 82%

Section: Pre-treatment and Post-treatment Of Datamentioning

confidence: 98%

Advances in two-dimensional correlation spectroscopy

Noda

2004

Vibrational Spectroscopy

235

149

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“…Two-dimensional IR correlation spectroscopy has been applied in protein researches to investigate whether the folding/unfolding process is fully cooperative or exhibits a sequential structure. To address this question, Fabian et al [36] performed a 2D correlation analysis on the IR spectra of the Cro-V55C dimmer of the λ Cro repressor, a small DNA-binding protein, one of the rare proteins whose thermal unfolding proceeds through stable equilibrium intermediates. This investigation demonstrated the capability of FTIR to detect a potential sequence of events in response to an external perturbation such as temperature.…”

Section: Resultsmentioning

confidence: 99%

Protein Structure and Function in the Time-Domain of Vibrational Spectroscopies. The Promising Applications of IR Synchrotron Radiation Micro-Spectroscopy

Marcelli

2006

Acta Phys. Pol. A

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Fourier Transform Infrared (FTIR) spectroscopy is a fundamental technique capable to characterize proteins and to investigate their conformation and dynamics in real physiological environments. Actually, a FTIR spectrum is characterized by many features, which may be correlated to the different components of the protein structure. In the last decade many relevant results have been achieved with this technique in terms of chemical imaging of proteins at subcellular level and in the investigation of cooperative phenomena. This contribution presents a few examples that illustrate the capability of the FTIR spectroscopy to investigate both protein structure and function and the opportunities offered by IR synchrotron radiation sources. Indeed the high source brilliance of these sources enables FTIR micro-spectroscopy to be performed with spatial and time resolution not available with standard sources. Moreover, the combination of synchrotron radiation and new two-dimensional detectors open new opportunities to investigate in the IR energy domain different protein processes in real time and with proteins in their native environments.

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“…This disulfide bridge does not perturb the basic Cro fold [9,10] with glutamine-16 replaced with leucine; FT-IR, Fourier transform infrared; DLS, dynamic light scattering; DSC, differential scanning calorimetry; CD, circular dichroism; NMR, nuclear magnetic resonance intermediate state [11][12][13]. Fourier transform infrared (FT-IR), dynamic light scattering (DLS) and differential scanning calorimetry (DSC) experiments revealed that the first thermal transition of the Cro-V55C dimer involves the unfolding of the three a-helices and the short b-strand in the N-terminal part of the protein [13][14][15]. This event is accompanied by the formation of tetramers.…”

Section: Introductionmentioning

confidence: 99%