NMR paper A general method for determining the electron self-exchange rates of blue copper prot

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[NMR paper] A general method for determining the electron self-exchange rates of blue copper prot

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NMR assignment:

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NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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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

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NOEs, other restraints:

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Pseudocontact shifts:

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SAVES2 or SAVES4

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NMR spectrum prediction:

FANDAS

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Backbone S2

Methyl S2

B-factor

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PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

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11-24-2010, 08:49 PM

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A general method for determining the electron self-exchange rates of blue copper prot

A general method for determining the electron self-exchange rates of blue copper proteins by longitudinal NMR relaxation.

Related Articles A general method for determining the electron self-exchange rates of blue copper proteins by longitudinal NMR relaxation.

J Am Chem Soc. 2002 Apr 17;124(15):4093-6

Authors: Jensen MR, Hansen DF, Led JJ

A general NMR method is presented that allows a precise determination of the second-order rate constant, k(ese), for the electron self-exchange in blue copper proteins, from the longitudinal relaxation rates of the nuclei in the protein. The method relies on the use of partly oxidized (paramagnetic) samples of the protein. In contrast to previous NMR approaches for the determination of electron self-exchange rates, the applicability of the method extends beyond the slow-exchange limit, k(ese)c

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