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

• Authors: A Marcelli
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

87.14.Ee; 87.15.Cc; 07.57.Ty; 07.85.Qe; 78.30.-j

Discipline

• 07.57.Ty: Infrared spectrometers, auxiliary equipment, and techniques
• 07.85.Qe: Synchrotron radiation instrumentation
• 78.30.-j: Infrared and Raman spectra(for vibrational states in crystals and disordered systems, see 63.20.-e and 63.50.-x, respectively; for Raman spectra of superconductors, see 74.25.nd)
• 87.15.Cc: Folding: thermodynamics, statistical mechanics, models, and pathways(see also 87.15.hm Folding dynamics)

• Publisher: Institute of Physics, Polish Academy of Sciences
• Journal: Acta Physica Polonica A
• Year: 2006
• Volume: 109
• Issue: 3
• Pages: 287-304

Dates

published

2006-03

received

2005-05-20

Contributors

author

A Marcelli

• INFN, Laboratori Nazionali di Frascati, P.O. Box 13, 00044 Frascati, Italy

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Identifiers

DOI

10.12693/APhysPolA.109.287