NMR paper Time dependence of aggregation in crystallizing lysozyme solutions probed using NMR s

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[NMR paper] Time dependence of aggregation in crystallizing lysozyme solutions probed using NMR s

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MDD

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Side-chains:

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Structure from NMR restraints:

Ab initio:

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Rosetta-NMR (Robetta)

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Fragment-based:

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Torsion angles from chemical shifts:

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TALOS

Promega- Proline

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CSI (via RCI server)

TALOS

MICS caps, β-turns

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PECAN

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RCI

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HADDOCK

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FANDAS

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Sparta+

Camshift

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ArShift- Aromatic

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CheShift-2- Cα

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Camcoil

Poulsen_rc_CS

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11-19-2010, 08:32 PM

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Time dependence of aggregation in crystallizing lysozyme solutions probed using NMR s

Time dependence of aggregation in crystallizing lysozyme solutions probed using NMR self-diffusion measurements.

Related Articles Time dependence of aggregation in crystallizing lysozyme solutions probed using NMR self-diffusion measurements.

Biophys J. 2001 Mar;80(3):1585-90

Authors: Price WS, Tsuchiya F, Arata Y

The time dependence of aggregation in supersaturated lysozyme solutions was studied using pulsed-gradient spin-echo NMR diffusion measurements as a function of lysozyme concentration at pH 6.0 and 298 K in the presence of 0.5 M NaCl. The measurements provide estimates of the weight-averaged diffusion coefficient of the monomeric to intermediate molecular weight lysozyme species present in the solution (very large aggregates and crystals are excluded from the average due to the NMR relaxation-weighting effects inherent in the method). The results show that the average molecular weight of the various lysozyme aggregates changed with sigmoidal kinetics and that these kinetics were strongly influenced by the initial lysozyme concentration. The visualization of the time dependence of the protein aggregation afforded by this method provides a deeper understanding of how the crystallizing conditions (especially the initial protein concentration) are related to the resulting crystals.

PMID: 11222319 [PubMed - indexed for MEDLINE]

Source: PubMed

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