NMR paper An adaptable phospholipid membrane mimetic system for solution NMR studies of membrane proteins.

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[NMR paper] An adaptable phospholipid membrane mimetic system for solution NMR studies of membrane proteins.

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Structure from NMR restraints:

Ab initio:

Fragment-based:

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GeNMR

I-TASSER

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Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

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TALOS

Promega- Proline

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TALOS

MICS caps, β-turns

d2D

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V-NMR

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Methyl S2

B-factor

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Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

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Shifty

Camcoil

Poulsen_rc_CS

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10-11-2017, 10:37 AM

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An adaptable phospholipid membrane mimetic system for solution NMR studies of membrane proteins.

An adaptable phospholipid membrane mimetic system for solution NMR studies of membrane proteins.

An adaptable phospholipid membrane mimetic system for solution NMR studies of membrane proteins.

J Am Chem Soc. 2017 Oct 09;:

Authors: Chien CH, Helfinger LR, Bostock MJ, Solt A, Tan YL, Nietlispach D

Abstract
Based on the saposin-A (SapA) scaffold protein we demonstrate the suitability of a size-adaptable phospholipid membrane-mimetic system for solution NMR studies of membrane proteins under close-to-native conditions. The Salipro nanoparticle size can be tuned over a wide pH range by adjusting the saposin-to-lipid stoichiometry enabling maintenance of sufficiently high amounts of phospholipid in the Salipro nanoparticle to mimic a realistic membrane environment while controlling the overall size to enable solution NMR for a range of membrane proteins. Three representative membrane proteins including one G-protein-coupled receptor (GPCR) were successfully incorporated into SapA-dimyristoylphosphatidylcholine (DMPC) nanoparticles and studied by solution NMR spectroscopy.

PMID: 28990386 [PubMed - as supplied by publisher]

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