NMR paper Orientational distribution of alpha-helices in the colicin B and E1 channel domains:

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[NMR paper] Orientational distribution of alpha-helices in the colicin B and E1 channel domains:

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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

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Amber

Structure from chemical shifts:

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Torsion angles from chemical shifts:

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Promega- Proline

Secondary structure from chemical shifts:

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TALOS

MICS caps, β-turns

d2D

PECAN

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RCI

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HADDOCK

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Pseudocontact shifts:

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FANDAS

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CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

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11-17-2010, 11:06 PM

nmrlearner

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Orientational distribution of alpha-helices in the colicin B and E1 channel domains:

Orientational distribution of alpha-helices in the colicin B and E1 channel domains: a one and two dimensional 15N solid-state NMR investigation in uniaxially aligned phospholipid bilayers.

Related Articles Orientational distribution of alpha-helices in the colicin B and E1 channel domains: a one and two dimensional 15N solid-state NMR investigation in uniaxially aligned phospholipid bilayers.

Biochemistry. 1998 Jan 6;37(1):16-22

Authors: Lambotte S, Jasperse P, Bechinger B

Thermolytic fragments of the channel-forming bacterial toxins colicin B and colicin E1 were uniformly labeled with the 15N isotope and reconstituted into uniaxially oriented membranes. These well-aligned samples were investigated by proton-decoupled 15N solid-state NMR spectroscopy at 40.5 and 71.0 MHz. The one dimensional spectra indicate a predominant orientation of the colicin alpha-helices parallel to the bilayer surface but also the presence of a considerable proportion of peptide bonds that align in a transmembrane direction. The orientational distribution of 15N-labeled amide bonds is nearly identical for colicin B and E1, each a representative of a different group of membrane-active colicins. This comparison indicates common structural features of the water-soluble as well as the bilayer-associated proteins. When the pH is lowered, the orientational distribution of amide vectors exhibits only a small shift from in-plane to transmembrane orientations, in agreement with increased affinity and activity of colicins at acidic conditions. The 15N spectral line shape was independent of the bilayer phospholipid composition (100-75 mol % phosphatidylcholine/0-25 mol % phosphatidylglycerol) or the protein-to-lipid ratio in the range 1.7 - 12 wt %. Two dimensional separated local field spectroscopy (PISEMA) resolves almost 200 15N resonances of the colicin B channel protein. Approximately 50 15N signals resonate in a region characteristic of transmembrane helical residues, in strong support of the previously suggested umbrella conformation of the closed colicin channel.

PMID: 9453746 [PubMed - indexed for MEDLINE]

Source: PubMed

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