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Spectroscopy - Volume 21 2007, Issue 3, Pages 143-149

Quantum Protein Centre, QuP, Department of Physics, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark



Copyright © 2007 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The Surface Enhanced Resonance Raman Scattering SERRS and Surface Enhanced Resonance Raman Optical Activity SERROA spectra of myoglobin and the myoglobin-azide complex were measured on very dilute samples 100 nM protein in order to analyze the sensitivity of SERROA spectroscopy when inducing small structural changes. While the SERRS spectra of the two compounds were virtually identical, comparison of the SERROA spectra revealed several differences, including frequency shifts and changes in signal intensity, consistent with structural change in the porphyrin prosthetic group of the protein upon azide complexation. Application of this method allows for rapid analysis of ligand binding in metalloproteins in dilute aqueous solution and could in the future, when combined with theoretical studies, increase the obtainable structural resolution of proteins beyond that of X-ray analysis.





Author: Christian Johannessen and Salim Abdali

Source: https://www.hindawi.com/



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