<<  February 2018  >>
 Mo  Tu  We  Th  Fr  Sa  Su 
     1  2  3  4
  5  6  7  8  91011
12131415161718
19202122232425
262728    

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

Site Statistics

mod_vvisit_countermod_vvisit_countermod_vvisit_countermod_vvisit_countermod_vvisit_countermod_vvisit_countermod_vvisit_countermod_vvisit_counter
mod_vvisit_counterToday172
mod_vvisit_counterYesterday430
mod_vvisit_counterThis week1730
mod_vvisit_counterLast week3557
mod_vvisit_counterThis month12335
mod_vvisit_counterLast month18915
mod_vvisit_counterAll1156595

Online (20 minutes ago): 10
Your IP: 54.227.17.101
,
Now is: 2018-02-22 10:55
Cytochromes c & b5
NMR spectroscopy was applied to study the conformational and electronic properties along with the stability of c- and b-type cytochromes from various sources (horse heart yeast and rat). NMR solution structures of horse heart cytochrome c ( PDB: 1GIW & 2GIW) and a variant of rat cytochrome b5 (PDB: 1MNY) have been determined and interesting redox-dependent or ligand dependent structural differences have been identified. These changes are thought to be related to the electron transfer process and conformational rearrangements of the heme propionic groups and key residues like Asn52 in cyt-c and Ser64 in cyt-b5 are considered as key residues for the functions of these proteins.