Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.

		BioNMR > Educational resources > Journal club
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.

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

01-22-2011, 01:52 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

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

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 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 state prior to aggregation. Based on a single real-time 2D (13)C-(13)C transition spectrum, kinetic information about the refolding and aggregation step could be extracted. In addition, structural rearrangements associated with refolding are estimated and several different aggregation scenarios were compared to the experimental data.

PMID: 21253842 [PubMed - as supplied by publisher]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Transient Enzyme–Substrate Recognition Monitored by Real-Time NMR Transient Enzyme–Substrate Recognition Monitored by Real-Time NMR Caroline Haupt, Rica Patzschke, Ulrich Weininger, Stefan Gro?ger, Michael Kovermann and Jochen Balbach http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2010048/aop/images/medium/ja-2011-010048_0002.gif Journal of the American Chemical Society DOI: 10.1021/ja2010048 http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/nknzYbs0FNE	nmrlearner	Journal club	0	06-30-2011 05:01 AM
Transient enzyme-substrate recognition monitored by real-time NMR. Transient enzyme-substrate recognition monitored by real-time NMR. Transient enzyme-substrate recognition monitored by real-time NMR. J Am Chem Soc. 2011 Jun 10; Authors: Haupt C, Patzschke R, Weininger U, Gröger S, Kovermann M, Balbach J Slow protein folding processes during which kinetic folding intermediates occur for an extended time can lead to aggregation and dysfunction in living cells. Therefore protein folding helpers have evolved, which prevent proteins from aggregation and/ or speed up folding processes. In this study we present the...	nmrlearner	Journal club	0	06-15-2011 01:15 PM
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
[NMR paper] Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic eve Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Related Articles Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. J Am Chem Soc. 2005 Jun 8;127(22):8014-5 Authors: Schanda P, Brutscher B We demonstrate for different protein samples that 2D 1H-15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle...	nmrlearner	Journal club	0	11-25-2010 08:21 PM
[NMR paper] Protein folding studied by real-time NMR spectroscopy. Protein folding studied by real-time NMR spectroscopy. Related Articles Protein folding studied by real-time NMR spectroscopy. Methods. 2004 Sep;34(1):65-74 Authors: Zeeb M, Balbach J Real-time NMR spectroscopy developed to a generally applicable method to follow protein folding reactions. It combines the access to high resolution data with kinetic experiments allowing very detailed insights into the development of the protein structure during different steps of folding. The present review concentrates mainly on the progress of real-time NMR...	nmrlearner	Journal club	0	11-24-2010 10:01 PM
[NMR paper] Folding of a beta-sheet protein monitored by real-time NMR spectroscopy. Folding of a beta-sheet protein monitored by real-time NMR spectroscopy. Related Articles Folding of a beta-sheet protein monitored by real-time NMR spectroscopy. J Mol Biol. 2003 May 16;328(5):1161-71 Authors: Mizuguchi M, Kroon GJ, Wright PE, Dyson HJ At low ionic strength, apoplastocyanin forms an unfolded state under non-denaturing conditions. The refolding of this state is sufficiently slow to allow real-time NMR experiments to be performed. Folding of apoplastocyanin, initiated by the addition of salt and followed by real-time 2D 1H-15N...	nmrlearner	Journal club	0	11-24-2010 09:01 PM
[NMR paper] Real-time NMR kinetic studies provide global and residue-specific information on the Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta. Related Articles Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta. J Mol Biol. 2003 May 2;328(3):693-703 Authors: Roy M, Jennings PA The interleukin-1beta (IL-1beta) structural motif is a beta-trefoil super fold created by six two-stranded beta-hairpins. Turns are thus...	nmrlearner	Journal club	0	11-24-2010 09:01 PM
[NMR paper] Following protein folding in real time using NMR spectroscopy. Following protein folding in real time using NMR spectroscopy. Related Articles Following protein folding in real time using NMR spectroscopy. Nat Struct Biol. 1995 Oct;2(10):865-70 Authors: Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative...	nmrlearner	Journal club	0	08-22-2010 03:50 AM

« 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