NMR paper Atomic-resolution monitoring of protein maturation in live human cells by NMR.

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[NMR paper] Atomic-resolution monitoring of protein maturation in live human cells by NMR.

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NMR assignment:

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Side-chains:

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Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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GeNMR

I-TASSER

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Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

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Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

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Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

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NOEs, other restraints:

Chemical shifts:

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Protein geomtery:

SAVES2 or SAVES4

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Backbone S2

Methyl S2

B-factor

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Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

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Protein disorder:

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Protein solubility:

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03-05-2013, 03:25 PM

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Atomic-resolution monitoring of protein maturation in live human cells by NMR.

Atomic-resolution monitoring of protein maturation in live human cells by NMR.

Atomic-resolution monitoring of protein maturation in live human cells by NMR.

Nat Chem Biol. 2013 Mar 3;

Authors: Banci L, Barbieri L, Bertini I, Luchinat E, Secci E, Zhao Y, Aricescu AR

Abstract
We use NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 oxidizes the SOD1 intrasubunit disulfide bond through both copper-dependent and copper-independent mechanisms. Our approach represents a new strategy for structural investigation of endogenously expressed proteins in a physiological (cellular) environment.

PMID: 23455544 [PubMed - as supplied by publisher]

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