NMR paper NMR conformational study of the cytoplasmic domain of the canine Sec61 gamma protein

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[NMR paper] NMR conformational study of the cytoplasmic domain of the canine Sec61 gamma protein

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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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08-22-2010, 02:20 PM

nmrlearner

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NMR conformational study of the cytoplasmic domain of the canine Sec61 gamma protein

NMR conformational study of the cytoplasmic domain of the canine Sec61 gamma protein from the protein translocation pore of the endoplasmic reticulum membrane.

Related Articles NMR conformational study of the cytoplasmic domain of the canine Sec61 gamma protein from the protein translocation pore of the endoplasmic reticulum membrane.

Biochemistry. 1996 Nov 26;35(47):14717-24

Authors: Beswick V, Baleux F, Huynh-Dinh T, KÃ©pÃ¨s F, Neumann JM, Sanson A

Conformational studies of the synthesized N-terminal cytoplasmic domain of the canine Sec61 gamma protein, an essential protein from the translocation pore of secretory proteins across the endoplasmic reticulum membrane, were performed using two-dimensional proton NMR spectroscopy. This canine domain is one of the smallest domains within the homologous protein family and may thus constitute the minimal functional structure. The peptide was solubilized in pure aqueous solution or in the presence of dodecylphosphocholine micelles mimicking a membrane-solution interface. In pure aqueous solution, the peptide is remarkably unfolded. Forming a stable complex with dodecylphosphocholine micelles, it acquires a well-defined alpha-helix-loop-alpha-helix secondary structure, with the helix, highly amphipathic, lying at the micelle surface. The loop comprising four residues is delimited by two flanking helix-capping structures, highly conserved in the whole homologous protein family. No tertiary structure, which could have been revealed by interhelix NOE contacts, was observed. From these experimental results and using general arguments based on sequence information and knowledge of peptide-membrane interactions, a structure of the entire Sec61 gamma protein in membrane bilayers is proposed.

PMID: 8942632 [PubMed - indexed for MEDLINE]

Source: PubMed

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