Journal Article

FZJ-2017-08113

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Low-Resolution Structure of Detergent-Solubilized Membrane Proteins from Small-Angle Scattering Data

Koutsioumpas, A. (Corresponding author)FZJ*

2017
Cell Press Cambridge, Mass.

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Please use a persistent id in citations: http://hdl.handle.net/2128/16156  doi:10.1016/j.bpj.2017.10.003

Abstract: Despite the ever-increasing usage of small-angle scattering as a valuable complementary method in the field of structural biology, applications concerning membrane proteins remain elusive mainly due to experimental challenges and the relative lack of theoretical tools for the treatment of scattering data. This fact adds up to general difficulties encountered also by other established methods (crystallography, NMR) for the study of membrane proteins. Following the general paradigm of ab initio methods for low-resolution restoration of soluble protein structure from small-angle scattering data, we construct a general multiphase model with a set of physical constraints, which, together with an appropriate minimization procedure, gives direct structural information concerning the different components (protein, detergent molecules) of detergent-solubilized membrane protein complexes. Assessment of the method’s precision and robustness is evaluated by performing shape restorations from simulated data of a tetrameric α-helical membrane channel (Aquaporin-0) solubilized by n-Dodecyl β-D-Maltoside and from previously published small-angle neutron scattering experimental data of the filamentous hemagglutinin adhesin β-barrel protein transporter solubilized by n-Octyl β-D-glucopyranoside. It is shown that the acquisition of small-angle neutron scattering data at two different solvent contrasts, together with an estimation of detergent aggregation number around the protein, permits the reliable reconstruction of the shape of membrane proteins without the need for any prior structural information.

Keyword(s): Health and Life (1st) ; Biology (2nd)

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Contributing Institute(s):

1. JCNS-FRM-II (JCNS (München) ; Jülich Centre for Neutron Science JCNS (München) ; JCNS-FRM-II)
2. Neutronenstreuung (Neutronenstreuung ; JCNS-1)

Research Program(s):

1. 6G15 - FRM II / MLZ (POF3-6G15) (POF3-6G15)
2. 6215 - Soft Matter, Health and Life Sciences (POF3-621) (POF3-621)
3. 6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623) (POF3-623)

Experiment(s):

1. No specific instrument

Appears in the scientific report 2017

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Database coverage:
; ; BIOSIS Previews ; Current Contents - Life Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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