NMR paper NMR studies of the dynamics of the multidomain protein urokinase-type plasminogen act

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[NMR paper] NMR studies of the dynamics of the multidomain protein urokinase-type plasminogen act

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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, 11:53 PM

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NMR studies of the dynamics of the multidomain protein urokinase-type plasminogen act

NMR studies of the dynamics of the multidomain protein urokinase-type plasminogen activator.

Related Articles NMR studies of the dynamics of the multidomain protein urokinase-type plasminogen activator.

Biochemistry. 1993 Jan 12;32(1):298-309

Authors: Nowak UK, Li X, Teuten AJ, Smith RA, Dobson CM

u-PA (urokinase-type plasminogen activator or urokinase) has been studied under a variety of solution conditions by 1-D and 2-D NMR spectroscopy. Very high quality spectra could be obtained from the recombinant protein despite the high molecular mass (46 kDa) by appropriate choice of solution conditions; mildly acidic pH and low ionic strength were found to be optimal. Comparison of spectra of u-PA with spectra of the isolated kringle and protease domains, the EGF-kringle pair, and a synthetic peptide from the kringle-protease linker region, enabled sequential assignments in the u-PA spectrum to be made for kringle resonances, and domain-specific assignments for many others. Simulations of line shapes in both 1-D and 2-D spectra enabled effective correlation times for the different domains, both isolated and in the intact protein, to be determined. These have permitted a model of the u-PA dynamics to be put forward involving extensive, but not unrestricted, motion between the different domains.

PMID: 8380336 [PubMed - indexed for MEDLINE]

Source: PubMed

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