Fine tuning the structure of the Cu2+ complex with the prion protein chicken repeat by proline isomerization.
The interaction between the single hexarepeat unit of chicken prion protein [ChPrP(54-59)] and Cu(II) was investigated by NMR, finding different coordination modes for the trans/trans and cis/trans isomers.
Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50-383 Wroclaw, Poland.
Paweł
P
Stańczak
Daniela
D
Valensin
Paulina
P
Juszczyk
Zbigniew
Z
Grzonka
Gianni
G
Valensin
Francesca
F
Bernardi
Elena
E
Molteni
Elena
E
Gaggelli
Henryk
H
Kozłowski
D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003300:Copper / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D009942:Organometallic Compounds / Q000737:chemistry*; D011328:Prions / Q000737:chemistry*; D011392:Proline / Q000737:chemistry*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012680:Sensitivity and Specificity; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D009942:Organometallic Compounds; D011328:Prions; D003300:Copper; D011392:Proline