NMR paper Populating the equilibrium molten globule state of apomyoglobin under conditions suit

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[NMR paper] Populating the equilibrium molten globule state of apomyoglobin under conditions suit

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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

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NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

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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

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NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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08-22-2010, 05:08 PM

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Populating the equilibrium molten globule state of apomyoglobin under conditions suit

Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR.

Related Articles Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR.

FEBS Lett. 1997 Nov 3;417(1):92-6

Authors: Eliezer D, Jennings PA, Dyson HJ, Wright PE

Conditions have been determined under which the equilibrium molten globule state of apomyoglobin is stable and remains monomeric for periods of time sufficient for the application of three-dimensional heteronuclear NMR experiments. The quality of initial two-dimensional NMR spectra suggests that sequence-specific assignments can be made for a majority of the protein resonances under these conditions. A pH titration of the protein followed using two-dimensional 1H-15N correlation experiments indicates that the equilibrium intermediate undergoes fast exchange on the chemical shift time scale with the unfolded state and intermediate time scale exchange with the native state, and suggests a strategy to assist with backbone resonance assignments. The conditions and techniques described may be applicable to the characterization of other equilibrium folding intermediates.

PMID: 9395082 [PubMed - indexed for MEDLINE]

Source: PubMed

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