| Autor: |
Beswick V; Département de Biologie Cellulaire et Moléculaire, URA CNRS 2096, Gif sur Yvette, France., Guerois R, Cordier-Ochsenbein F, Coïc YM, Tam HD, Tostain J, Noël JP, Sanson A, Neumann JM |
| Jazyk: |
angličtina |
| Zdroj: |
European biophysics journal : EBJ [Eur Biophys J] 1999; Vol. 28 (1), pp. 48-58. |
| DOI: |
10.1007/s002490050182 |
| Abstrakt: |
To further examine to what extent a dodecyl-phosphocholine (DPC) micelle mimics a phosphatidylcholine bilayer environment, we performed 13C, 2H, and 31P NMR relaxation measurements. Our data show that the dynamic behavior of DPC phosphocholine groups at low temperature (12 degrees C) corresponds to that of a phosphatidylcholine interface at high temperature (51 degrees C). In the presence of helical peptides, a PMP1 fragment, or an annexin fragment, the DPC local dynamics are not affected whereas the DPC aggregation number is increased to match an appropriate area/volume ratio for accommodating the bound peptides. We also show that quantitative measurements of paramagnetic relaxation enhancements induced by small amounts of spin-labeled phospholipids on peptide proton signals provide a meaningful insight on the location of both PMP1 and annexin fragments in DPC micelles. The paramagnetic contributions to the relaxation were extracted from intra-residue cross-peaks of NOESY spectra for both peptides. The location of each peptide in the micelles was found consistent with the corresponding relaxation data. As illustrated by the study of the PMP1 fragment, paramagnetic relaxation data also allow us to supply the missing medium-range NOEs and therefore to complete a standard conformational analysis of peptides in micelles. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
