NMR paper Hydration-optimized oriented phospholipid bilayer samples for solid-state NMR structu

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[NMR paper] Hydration-optimized oriented phospholipid bilayer samples for solid-state NMR structu

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

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SAVES2 or SAVES4

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Methyl S2

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Shiftx2

Sparta+

Camshift

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ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

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NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

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11-24-2010, 09:01 PM

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Hydration-optimized oriented phospholipid bilayer samples for solid-state NMR structu

Hydration-optimized oriented phospholipid bilayer samples for solid-state NMR structural studies of membrane proteins.

Related Articles Hydration-optimized oriented phospholipid bilayer samples for solid-state NMR structural studies of membrane proteins.

J Magn Reson. 2003 Mar;161(1):64-9

Authors: Marassi FM, Crowell KJ

The preparation of oriented, hydration-optimized lipid bilayer samples, for NMR structure determination of membrane proteins, is described. The samples consist of planar phospholipid bilayers, containing membrane proteins, that are oriented on single pairs of glass slides, and are placed in the coil of the NMR probe with the bilayer plane perpendicular to the direction of the magnetic field. Lipid bilayers provide a medium that closely resembles the biological membrane, and sample orientation both preserves the intrinsic membrane-defined directional quality of membrane proteins, and provides the mechanism for resonance line narrowing. The hydration-optimized samples overcome some of the difficulties associated with multi-dimensional, high-resolution, solid-state NMR spectroscopy of membrane proteins. These samples have greater stability over the course of multi-dimensional NMR experiments, they have lower sample conductance for greater rf power efficiency, and enable greater rf coil filling factors to be obtained for improved experimental sensitivity. Sample preparation is illustrated for the membrane protein CHIF (channel inducing factor), a member of the FXYD family of ion transport regulators.

PMID: 12660112 [PubMed - indexed for MEDLINE]

Source: PubMed

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