title: Combined use of optical spectroscopy and computational methods to study the binding and the photoinduced conformational modification of proteins when NMR and X-ray structural determinations are not an option.
abstract: The functions of proteins depend on their interactions with various ligands and these interactions are controlled by the structure of the polypeptides. If one can manipulate the structure of proteins, their functions can in principle be modulated. The issue of protein structure-function relationship is not only a central problem in biophysics, but is becoming clear that the ability to "artificially" modify the structure of proteins could be relevant in fields beyond the biomedical area to provide, for instance, light responses in proteins which would not possess such properties in their native state. This chapter presents an overview of the combination of optical electronic and vibrational spectroscopy with various computational methods to investigate the binding between photoactive ligands and proteins.
authors.affiliation: Department of Physics and Astronomy, The University of Texas at San Antonio, San Antonio, Texas, USA. Electronic address: Lorenzo.Brancaleon@utsa.edu.
authors.forename: Lorenzo
authors.initials: L
authors.lastname: Brancaleon
mesh_terms: D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010455:Peptides / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry; D014965:X-Rays
chemical_list: D008024:Ligands; D010455:Peptides; D011506:Proteins
keywords: Density functional theory; Docking simulations; Fluorescence spectroscopy; Ligand binding; Resonance Raman spectroscopy