NMR paper 1H NMR-based absolute quantitation of human lipoproteins and their lipid contents dir

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[NMR paper] 1H NMR-based absolute quantitation of human lipoproteins and their lipid contents dir

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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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08-22-2010, 03:29 AM

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1H NMR-based absolute quantitation of human lipoproteins and their lipid contents dir

1H NMR-based absolute quantitation of human lipoproteins and their lipid contents directly from plasma.

Related Articles 1H NMR-based absolute quantitation of human lipoproteins and their lipid contents directly from plasma.

J Lipid Res. 1994 Dec;35(12):2292-304

Authors: Ala-Korpela M, Korhonen A, Keisala J, HÃ¶rkkÃ¶ S, Korpi P, Ingman LP, Jokisaari J, Savolainen MJ, KesÃ¤niemi YA

A new method is presented for absolute quantitation of lipid and protein contents of human lipoproteins directly from plasma. The method enables complete lipoprotein lipid profiles to be obtained in a total time of less than one hour. Absolute concentrations of triglycerides, phospholipids, total cholesterol, free cholesterol, esterified cholesterol, total proteins, and total masses can be estimated for the very low density (VLDL) and low density (LDL) lipoprotein fractions. For the high density lipoprotein (HDL) fraction all components except triglycerides can be quantitated. The method is a combination of 1H NMR spectroscopy and a sophisticated lineshape fitting analysis technique. In this paper we present the calibration of the method using 15 plasma samples followed by a double-blind test of 51 plasma samples from 43 individuals. In total, 66 plasma samples were analyzed. Comparison of the 1H NMR-based results with the data of the biochemical assays showed excellent agreement; the correlation coefficient for VLDL triglycerides was 0.98, for LDL cholesterol 0.88, and for HDL cholesterol 0.93. This method can be directly integrated to many kinds of biomedical NMR studies to offer additional biochemically important quantitative lipoprotein information, the measurement of which is usually too laborious by conventional biochemical methods and too high-priced to be adapted into the study protocols. Moreover, the method also has considerable potential to be developed for a routine clinical assay.

PMID: 7897326 [PubMed - indexed for MEDLINE]

Source: PubMed

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