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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.

Stanczak, P., Valensin, D., Juszczyk, P., Grzonka, Z., Valensin, G., Bernardi, F., et al. (2005). Fine tuning the structure of the Cu2+ complex with the prion protein chicken repeat by proline isomerization. CHEMICAL COMMUNICATIONS, 26, 3298-3300 [10.1039/b504986e].

Fine tuning the structure of the Cu2+ complex with the prion protein chicken repeat by proline isomerization

Valensin, Daniela;Valensin, Gianni;Gaggelli, Elena;
2005-01-01

Abstract

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.
2005
CHEMICAL COMMUNICATIONS
Stanczak, P., Valensin, D., Juszczyk, P., Grzonka, Z., Valensin, G., Bernardi, F., et al. (2005). Fine tuning the structure of the Cu2+ complex with the prion protein chicken repeat by proline isomerization. CHEMICAL COMMUNICATIONS, 26, 3298-3300 [10.1039/b504986e].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/18608
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