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Contact details

Georgios A. Spyroulias, PhD.
Department of Pharmacy
University of Patras
Panepistimioupoli-Rion,
GR-26504 Patras, GREECE
Tel:    +30.2610.969950 (office)
+30.2610.969951 (terra silico)
+30.2610.969952 (terra vitro)
Fax:    +30.2610.969950
Email:  G.A.Spyroulias@upatras.gr

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Now is: 2017-11-21 21:24
nmrstudiesThe pioneering work of two physicists, Felix Bloch and Edward Purcell, and their collaborators that were studying the behavior of magnetic nuclei in a magnetic field led to the foundation of a new field, that of NMR, in 1946. They showed that certain magnetic nuclei can adopt nuclear-spin states of different energy, and can be induced to flip between these states by the application of radio-frequency radiation. Such magnetic nuclei are among others 1H, 13C and 15N which are found in different amounts of natural abundance in many chemicals, and especially in biological macromolecules like peptides, proteins, RNA, DNA etc.

The chemical environment of a particular magnetic nucleus in a molecule determines its NMR properties, such as the energy difference between the orientations and consequently the frequency at which that nucleus absorbs energy (its resonance frequency). Magnetic nuclei are affected by each other as well as the applied field, both through chemical bonds (spin–spin coupling) and over short distances through space (dipole–dipole coupling). The nature of the coupling can thus be exploited to assign resonance signals to particular nuclei in a structure, and derive constraints for the distances separating them.

On the basis of these fundamental properties, NMR has evolved into an important technique in chemistry and the life sciences and with the synergistic action of molecular biology has become a standard method for macromolecular 3D structure determination. Notably, NMR is currently the only technique which can solve structures of proteins and peptides in solution with atomic-level resolution. There are currently more than 8000 NMR structures deposited in Protein Data Bank and Biomolecular NMR is an essential component in the research activities of the current structural and functional genomics initiatives all over the world.
In our laboratory multinuclear and multidimensional NMR spectroscopy is applied to uniformly isotope-labeled polypeptides (increased % of 13C and 15N nuclei) which enable the assignment process through sequential assignment. Geometrical information is extracted from NOE-based experiments and is used as input data to the conformational study and structure determination of biomolecules (proteins and peptides). The aim is to gain atomic level insights about the architecture of proteins and their assembly in protein complexes with ligands/substrates or drug candidates and to link these data with the function. Additionally, mobility is an essential physical property of biomolecules providing invaluable information on molecular recognition processes. Structure in concert with dynamics can offer a profound view on protein's function.