NMR paper The detection of proline isomerase activity in FK506-binding protein by two-dimension

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[NMR paper] The detection of proline isomerase activity in FK506-binding protein by two-dimension

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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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08-21-2010, 11:04 PM

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The detection of proline isomerase activity in FK506-binding protein by two-dimension

The detection of proline isomerase activity in FK506-binding protein by two-dimensional 1H NMR exchange spectroscopy.

Related Articles The detection of proline isomerase activity in FK506-binding protein by two-dimensional 1H NMR exchange spectroscopy.

Biochem Biophys Res Commun. 1990 Aug 31;171(1):445-50

Authors: Justice RM, Kline AD, Sluka JP, Roeder WD, Rodgers GH, Roehm N, Mynderse JS

1H NMR assignments of the trans and cis isomers of succinyl-Ala-Ala-Pro-Phe-p-nitroanilide were accomplished by two-dimensional NMR techniques. Conformational exchange between the cis and trans isomers was not detected in the two-dimensional exchange spectra (NOESY) until catalytic amounts of FK506-binding protein (FKbp) were added. The addition of FK506 to the enzyme-substrate solution inhibited the enzyme and removed the substrate exchange peaks.

PMID: 1697463 [PubMed - indexed for MEDLINE]

Source: PubMed

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