NMR paper Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.

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[NMR paper] Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.

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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

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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08-30-2014, 11:00 PM

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Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.

Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.

Related Articles Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.

Biochim Biophys Acta. 2014 Aug 25;

Authors: Laage S, Tao Y, McDermott AE

Abstract
The interaction of lipids with subunit c from F1Fo ATP synthase are studied by biophysical methods. Subunit c from both Escherichia coli and Streptococcus pneumoniae interact and copurify with cardiolipin. Solid state NMR data on oligomeric rings of Fo show that the cardiolipin interacts with the c subunits in membrane bilayers. These studies offer strong support for the hypothesis that Fo has specific interactions with cardiolipin. This article is part of a Special Issue entitled: NMR Spectroscopy for Atomistic Views of Biomembranes and Cell Surfaces.

PMID: 25168468 [PubMed - as supplied by publisher]

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