Abstract

Characterizing the structure of membrane proteins (MPs) generally requires extraction from their native environment, most commonly with detergents. Yet, the physicochemical properties of detergent micelles and lipid bilayers differ markedly and could alter the structural organization of MPs, albeit without general rules. Dodecylphosphocholine (DPC) is the most widely used detergent for MP structure determination by NMR, but the physiological relevance of several prominent structures has been questioned, though indirectly, by other biophysical techniques, e.g., functional/thermostability assay (TSA) and molecular dynamics (MD) simulations. Here, we resolve unambiguously this controversy by probing the functional relevance of three different mitochondrial carriers (MCs) in DPC at the atomic level, using an exhaustive set of solution-NMR experiments, complemented by functional/TSA and MD data. Our results provide atomic-level insight into the structure, substrate interaction and dynamics of the detergent−membrane protein complexes and demonstrates cogently that, while high-resolution NMR signals can be obtained for MCs in DPC, they systematically correspond to nonfunctional states .

Autore Pugliese

• Capobianco Loredana

Tutti gli autori

• Kurauskas V. , Hessel A. , Ma P. , Lunetti P. , Weinhaupl K. , Imbert L. , Brutscher B. , King M. S. , Sounier R. , Dolce V. , Kunji E.R. S. , Capobianco L. , Chipot C. , Dehez F. , Bersch B. , Schanda P.

Titolo volume/Rivista

THE JOURNAL OF PHYSICAL CHEMISTRY LETTERS

Anno di pubblicazione

2018

ISSN

1948-7185

ISBN

Non Disponibile

Numero di citazioni Wos

Nessuna citazione

Ultimo Aggiornamento Citazioni

Non Disponibile

Numero di citazioni Scopus

1

Ultimo Aggiornamento Citazioni

26/04/2018

Settori ERC

Non Disponibile

Codici ASJC

Non Disponibile