Conformational Studies of Proteins and Peptides

Dear Colleagues,

Proteins and linear heteropolymers, the backbone of which is formed by successive peptide bonds between natural amino acids, provide a wealth of structural properties. Despite the fact that the conformational flexibility of each polymer residue is simply governed by three torsion angles (f, y, w), a variety of forms is expected in relation to the values assigned to these angles (helices, sheets, and turns, etc.). With structure and function being closely related in proteins, the global conformation adopted by a peptide chain determines its function. The surrounding water molecules and their dynamics also play a pivotal role in the chain folding of globular proteins, in maintaining the disordered character of chains, and in inducing their aggregation processes, which are known as the main cause of several human diseases such as Alzheimer’s, Parkinson’s and type‑II diabetes. Short size peptide chains are recognized as efficient bioactive, functional and imaging agents. Their versatility for elaborating therapeutic agents, used, for instance, as analogues of natural hormones, as well for as innovating synthetic materials has been emphasized over the past two decades. In this Special Issue, our aim is to explore the capability of different physical techniques such as X-ray diffraction/scattering, NMR, optical spectroscopies (electronic circular dichroism, FT-IR absorption, vibrational circular dichroism, Raman scattering, Raman optical activity), in combination with adequate theoretical methods, to elucidate the structural features of proteins and peptides.

Prof. Dr. Mahmoud Ghomi
Dr. Santiago Sanchez-Cortés
Dr. Belén Hernández
Guest Editors

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