NMR paper Assignment of oriented sample NMR resonances from a three transmembrane helix protein.

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[NMR paper] Assignment of oriented sample NMR resonances from a three transmembrane helix protein.

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NMR processing:

MDD

NMR assignment:

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Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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I-TASSER

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Amber

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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

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RCI

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NOEs, other restraints:

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Pseudocontact shifts:

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SAVES2 or SAVES4

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Methyl S2

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PPM

CheShift-2- Cα

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Camcoil

Poulsen_rc_CS

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02-11-2014, 09:58 PM

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Assignment of oriented sample NMR resonances from a three transmembrane helix protein.

Assignment of oriented sample NMR resonances from a three transmembrane helix protein.

Related Articles Assignment of oriented sample NMR resonances from a three transmembrane helix protein.

J Magn Reson. 2014 Jan 21;240C:34-44

Authors: Murray DT, Hung I, Cross TA

Abstract
Oriented sample solid state NMR techniques have been routinely employed to determine the structures of membrane proteins with one or two transmembrane helices. For larger proteins the technique has been limited by spectral resolution and lack of assignment strategies. Here, a strategy for resonance assignment is devised and applied to a three transmembrane helix protein. Sequence specific assignments for all labeled transmembrane amino acid sites are obtained, which provide a set of orientational restraints and helix orientations in the bilayer. Our experiments expand the utility of solid state NMR in membrane protein structure characterization to three transmembrane helix proteins and represent a straightforward strategy for routinely characterizing multiple transmembrane helix protein structures.

PMID: 24509383 [PubMed - as supplied by publisher]

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