NMR paper Protein folding monitored at individual residues during a two-dimensional NMR experim

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[NMR paper] Protein folding monitored at individual residues during a two-dimensional NMR experim

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NMR assignment:

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Side-chains:

NOEs:

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:

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

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NOEs, other restraints:

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Methyl S2

B-factor

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Shiftx2

Sparta+

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ArShift- Aromatic

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Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

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NMR sample preparation:

Protein disorder:

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Protein solubility:

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08-22-2010, 02:20 PM

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Protein folding monitored at individual residues during a two-dimensional NMR experim

Protein folding monitored at individual residues during a two-dimensional NMR experiment.

Related Articles Protein folding monitored at individual residues during a two-dimensional NMR experiment.

Science. 1996 Nov 15;274(5290):1161-3

Authors: Balbach J, Forge V, Lau WS, van Nuland NA, Brew K, Dobson CM

An approach is described to monitor directly at the level of individual residues the formation of structure during protein folding. A two-dimensional heteronuclear nuclear magnetic resonance (NMR) spectrum was recorded after the rapid initiation of the refolding of a protein labeled with nitrogen-15. The intensities and line shapes of the cross peaks in the spectrum reflected the kinetic time course of the folding events that occurred during the spectral accumulation. The method was used to demonstrate the cooperative nature of the acquisition of the native main chain fold of apo bovine alpha-lactalbumin. The general approach, however, should be applicable to the investigation of a wide range of chemical reactions.

PMID: 8895458 [PubMed - indexed for MEDLINE]

Source: PubMed

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