NMR paper Binding of 1-methylimidazole to cytochrome c: kinetic analysis and resonance assignme

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[NMR paper] Binding of 1-methylimidazole to cytochrome c: kinetic analysis and resonance assignme

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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, 03:41 AM

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Binding of 1-methylimidazole to cytochrome c: kinetic analysis and resonance assignme

Binding of 1-methylimidazole to cytochrome c: kinetic analysis and resonance assignments by two-dimensional NMR.

Related Articles Binding of 1-methylimidazole to cytochrome c: kinetic analysis and resonance assignments by two-dimensional NMR.

Biochim Biophys Acta. 1995 Apr 27;1248(2):177-85

Authors: Shao W, Liu G, Tang W

The binding of 1-methylimidazole to the heme iron by displacing Met-80 of cytochrome c has been studied by two-dimensional (2D) exchange spectroscopy. Two components of cytochrome c ligated by 1-methylimidazole (1-MeIm-cyt c) are first identified, which are related to the sterically hindered orientation of 1-methylimidazole by the heme pocket. Based on a matrix formalism, the kinetic parameters are calculated from the 2D peak amplitudes. With the known resonance assignments of cytochrome c, some hyperfine shifted resonances arising from heme peripheral protons and two axial ligands, and some side-chain resonances of the aliphatic and aromatic protons of 1-MeIm-cyt c have been straightforwardly assigned, which provide a clue to ligand-induced electronic and molecular structural changes of the protein.

PMID: 7748900 [PubMed - indexed for MEDLINE]

Source: PubMed

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