Vibrational Spectroscopy as a Versatile Tool To Predict Protein Structure

Dear Colleagues,

It is a great pleasure to announce this Special Issue on “Vibrational Spectroscopy as a Versatile Tool To Predict Protein Structure”.

Protein structure has been investigated for more than four decades by means of vibrational spectroscopy: the specific band assignments (i.e., marker bands of amino acid side chains, disulfide bridge conformation, metal coordination) and signatures of the secondary structure have been established. The assignments are usually based on model compounds (e.g., amino acids or short peptides) and may be universal for the whole class of molecules (i.e., amide bands of proteins are assigned to polypeptide backbone modes).

Moreover, information on the presence of some functional moieties (such as –SH, S–S, etc.), the microenvironment of some amino acid residues (such as Tyr), the strength of hydrogen bonding, and the interaction between charged side chains (i.e., NH₃⁺, COO⁻) or between metal ions and amino acids can be obtained.

It is well known that protein function is directly related to the resulting 3D structure and, therefore, vibrational techniques were used to monitor structural changes in many different situations:

    -  After adsorption on a surface (i.e., the case of the biomimetic approach on biomaterials surface), studying also the adsorbed–adsorbent interactions (covalent, electrostatic, chemical bonds formation, hydrogen and van der Waals bonds, hydrophobic and hydrophilic interactions);

    -  In denaturing conditions (i.e. after heating and/or pH changes);

    -  After interaction with other molecules (biomolecules as cellular membranes or grafting agents that can modify the properties of materials of proteinaceous origin);

    -  In physiological processes (i.e. the mineralization of collagen fibers, under free radical stress).

The study of metal-to-protein binding sites has been widely carried out by means of Raman resonance conditions and, in many cases, decades before the determination of protein structure by X-rays or NMR techniques.

More recently, surface-enhanced Raman scattering (SERS) on noble metal colloids has been successfully applied to the study of proteins in aqueous systems at very low concentrations (thus, similar to the physiological environment).

Prof. Dr. Paola Taddei
Dr. Michele Di Foggia
Guest Editors

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