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

		BioNMR > Educational resources > Journal club
[NMR paper] Time dependence of aggregation in crystallizing lysozyme solutions probed using NMR s

Webservers

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:

Thread Tools

Search this Thread

Rate Thread

Display Modes

11-19-2010, 08:32 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,731

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

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

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[Question from NMRWiki Q&A forum] bulk water relaxation dependence on temperature bulk water relaxation dependence on temperature Is liquid water's relaxation rate strongly dependent on temperature, and does anyone have a link to a good online article with the dependency equation?Thanks! Check if somebody has answered this question on NMRWiki QA forum	nmrlearner	News from other NMR forums	0	12-23-2011 10:21 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy Abstract It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate...	nmrlearner	Journal club	0	01-27-2011 04:31 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. J Biomol NMR. 2011 Jan 21; Authors: Etzkorn M, Böckmann A, Baldus M It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all...	nmrlearner	Journal club	0	01-22-2011 01:52 PM
NMR Detection of an Equilibrium Phase Consisting of Monomers and Clusters in Concentrated Lysozyme Solutions. NMR Detection of an Equilibrium Phase Consisting of Monomers and Clusters in Concentrated Lysozyme Solutions. Related Articles NMR Detection of an Equilibrium Phase Consisting of Monomers and Clusters in Concentrated Lysozyme Solutions. J Phys Chem B. 2010 Dec 2; Authors: Barhoum S, Yethiraj A Protein aggregation is an important biophysical phenomenon, and it is technically challenging to quantify. Scattering studies in concentrated protein solutions are not in complete agreement over the existence of an equilibrium cluster phase. We use...	nmrlearner	Journal club	0	12-04-2010 07:24 PM
[NMR paper] A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR experiment and quantum chemical calculations. Related Articles A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR experiment and quantum chemical calculations. J Biomol NMR. 2005 Feb;31(2):87-95 Authors: Ko?mi?ski W, Zhukov I, Pecul M, Sadlej J A new pulse sequence exploiting double- and zero-quantum evolution of two-spin 15N-13C' coherence is proposed for the accurate measurements of 2J(N(i),C alpha(i-1)) coupling...	nmrlearner	Journal club	0	11-24-2010 11:14 PM
Ekaterina Heldwein: Crystallizing killers Ekaterina Heldwein: Crystallizing killers - Scientist http://nt3.ggpht.com/news/tbn/M8FKwvw_sSQ0mM/6.jpg Scientist <img alt="" height="1" width="1" /> Ekaterina Heldwein: Crystallizing killers Scientist 1 Using X-ray crystallography, electron microscopy, and nuclear magnetic resonance spectroscopy to determine a protein's three-dimensional structure, ...	nmrlearner	NMR research groups	0	09-29-2010 10:40 PM
Conformational dependence of 13C shielding and coupling constants for methionine Abstract Methionine residues fulfill a broad range of roles in protein function related to conformational plasticity, ligand binding, and sensing/mediating the effects of oxidative stress. A high degree of internal mobility, intrinsic detection sensitivity of the methyl group, and low copy number have made methionine labeling a popular approach for NMR investigation of selectively labeled protein macromolecules. However, selective labeling approaches are subject to more limited information content. In order to optimize the information available from such studies, we have performed DFT...	nmrlearner	Journal club	0	08-25-2010 03:51 PM
[NMR paper] pH dependence of the absorbance and 31P NMR spectra of O-acetylserine sulfhydrylase i pH dependence of the absorbance and 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine. Related Articles pH dependence of the absorbance and 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine. Biochemistry. 1992 Mar 3;31(8):2298-303 Authors: Cook PF, Hara S, Nalabolu S, Schnackerz KD O-Acetylserine sulfhydrylase (OASS) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme which catalyzes the final step in the biosynthesis of L-cysteine in Salmonella, viz.,...	nmrlearner	Journal club	0	08-21-2010 11:41 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off