Atomic resolution view into the structure–function relationships of the human myelin peripheral membrane protein P2

Ruskamo, S.; Yadav, R.P.; Sharma, S.; Lehtimäki, M.; Laulumaa, S.; Aggarwal, S.; Simons, M.; Bürck, J.; Ulrich, A.S.; Juffer, A.H.; Kursula, I.; Kursula, P.

doi:10.1107/S1399004713027910

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 7
CD analysis of P2. (a) CD spectra in buffer (dashed line) and in DMPC/DMPG liposomes (1:150 protein:lipid, thin line). The difference spectrum between these samples is shown as a dotted line and the OCD spectrum of P2 in oriented membranes is shown as a thick line. (b, c) Thermal stability of P2 in solution (b) and of membrane-bound P2 (c). For clarity, CD spectra are shown at intervals of 10 K from 293 to 363 K.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 1| December 2014| Pages 165-176

doi:10.1107/S1399004713027910

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