NMR paper NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF bind

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[NMR paper] NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF bind

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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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11-19-2010, 08:32 PM

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NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF bind

NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF binding protein-5 (IGFBP-5) determined free in solution and in complex with IGF-II.

Related Articles NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF binding protein-5 (IGFBP-5) determined free in solution and in complex with IGF-II.

Eur J Biochem. 2001 Feb;268(4):1058-65

Authors: Renner C, Holak T

15N NMR relaxation rates of mini-IGFBP-5, an N-terminal insulin-like growth factor binding domain of the insulin-like growth factor binding protein 5 (IGFBP-5), were analysed at three field strengths using the Lipari-Szabo procedure (see below) and reduced spectral density methods. Isotropic and anisotropic Lipari-Szabo models were analysed and an analytical formula for the overall correlation time for anisotropic molecules is presented. Mini-IGFBP-5 was found to be mainly rigid on fast ps time scales except for 11 unstructured flexible residues at the C-terminus. The insulin-like growth factor binding loop in the apo-protein exhibits small amounts of flexibility on fast time scales (ps to ns) but several loop residues show significant exchange broadening. These loop residues display no exchange broadening in the complex of IGF-II/mini-IGFBP-5. The isotropic overall tumbling time in solution at 31 degrees C of mini-IGFBP-5 complexed to IGF-II is tauc = 18.4 +/- 0.2 ns indicating a strong tendency for aggregation.

PMID: 11179972 [PubMed - indexed for MEDLINE]

Source: PubMed

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