NMR paper Magnetic susceptibility to measure total protein concentration from NMR metabolite spectra: Demonstration on blood plasma.

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[NMR paper] Magnetic susceptibility to measure total protein concentration from NMR metabolite spectra: Demonstration on blood plasma.

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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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03-19-2014, 10:43 PM

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Magnetic susceptibility to measure total protein concentration from NMR metabolite spectra: Demonstration on blood plasma.

Related Articles Magnetic susceptibility to measure total protein concentration from NMR metabolite spectra: Demonstration on blood plasma.

Magn Reson Med. 2014 Mar 17;

Authors: Jupin M, Michiels PJ, Girard FC, Wijmenga SS

Abstract
PURPOSE: Accurate metabolite and protein quantification in blood plasma and other body fluids from one single NMR measurement, allowing for improved quantitative metabolic profiling and better assessment of metabolite-protein interactions.
THEORY AND METHODS: The total protein concentration is derived from the common chemical-shift changes-caused by protein-induced bulk magnetic susceptibility (BMS)-measured on well-accessible and exchange-free metabolite resonances. These BMS shifts are simply obtained by external referencing with respect to 3-(trimethylsilyl)propionic-2,2,3,3-d4 acid, sodium salt in a coaxial insert.
RESULTS: Based on blood-plasma data from five volunteers, the estimated accuracy of the BMS method is 10 g/L). Also, it allows measurement of the presence and sign of exchange-induced chemical-shift changes. Magn Reson Med, 2014. © 2014 Wiley Periodicals, Inc.

PMID: 24639074 [PubMed - as supplied by publisher]

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