TY  - JOUR
AU  - Koutsioumpas, Alexandros
AU  - Berthaud, Alice
AU  - Mangenot, Stephanie
AU  - Perez, Javier
TI  - Ab Initio and All-Atom Modeling of Detergent Organization around Aquaporin-0 Based on SAXS Data
JO  - The journal of physical chemistry  / B
VL  - 117
IS  - 43
SN  - 1520-5207
CY  - Washington, DC
PB  - Soc.
M1  - FZJ-2013-04727
SP  - 13588–13594
PY  - 2013
AB  - A necessary initial step for the application of small angle X-ray scattering (SAXS) as an analytical probe for structural investigations of membrane proteins in solution is the precise knowledge of the structure of spontaneously formed detergent assemblies around the protein. Following our recent article (Berthaud et al. J. Am. Chem. Soc. 2012, 134, 10080–10088) on the study of the n-dodecyl β-d-maltopyranoside (dDM) corona surrounding Aquaporin-0 tetramers in solution, we aimed at the development of more elaborate models, exploiting the information content of the scattering data. Two additional approaches are developed here for the fit of SAXS experimental data, one based on a generalized ab initio algorithm for the construction of a coarse-grained representation of the detergent assemblies, and a second based on atomistic molecular dynamics. Accordingly, we are able to fit the SAXS experimental data and obtain a better insight concerning the structure of the detergent corona around the hydrophobic part of the Aquaporin-0 surface. The present analysis scheme represents an additional step toward future conformational studies of transmembrane proteins in solution.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000326608500022
C6  - pmid:24144436
DO  - DOI:10.1021/jp407688x
UR  - https://juser.fz-juelich.de/record/138629
ER  -