Hydrodynamic dispersion in [Formula: see text] -lactoglobulin gels measured by PGSE NMR.

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Hydrodynamic dispersion in [Formula: see text] -lactoglobulin gels measured by PGSE NMR.

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NMR processing:

MDD

NMR assignment:

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Side-chains:

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Structure from NMR restraints:

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Fragment-based:

Rosetta-NMR (Robetta)

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GeNMR

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Amber

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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

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RCI

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HADDOCK

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B-factor

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Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

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CCPN

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DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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03-02-2011, 11:54 AM

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Hydrodynamic dispersion in [Formula: see text] -lactoglobulin gels measured by PGSE NMR.

Hydrodynamic dispersion in [Formula: see text] -lactoglobulin gels measured by PGSE NMR.

Hydrodynamic dispersion in [Formula: see text] -lactoglobulin gels measured by PGSE NMR.

Eur Phys J E Soft Matter. 2011 Feb;34(2):1-15

Authors: Fridjonsson EO, Bernin D, Seymour JD, Nydén M, Codd SL

The displacement scale dependent molecular dynamics of solvent water molecules flowing through [Formula: see text] -lactoglobulin gels are measured by pulse gradient spin echo (PGSE) nuclear magnetic resonance (NMR). Gels formed under different p H conditions generate structures which are characterized by magnetic resonance imaging (MRI) and PGSE NMR measured dynamics as homogeneous and heterogeneous. The data presented clearly demonstrate the applicability of the theoretical framework for modeling hydrodynamic dispersion to the analysis of protein gels.

PMID: 21359931 [PubMed - in process]

Source: PubMed

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