NMR paper NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins.

		BioNMR > Educational resources > Journal club
[NMR paper] NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins.

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

03-24-2015, 09:58 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

NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins.

NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins.

J Magn Reson. 2015 Apr;253:60-70

Authors: Ravera E, Schubeis T, Martelli T, Fragai M, Parigi G, Luchinat C

Abstract
Resolution and sensitivity in solid state NMR (SSNMR) can rival the results achieved by solution NMR, and even outperform them in the case of large systems. However, several factors affect the spectral quality in SSNMR samples, and not all systems turn out to be equally amenable for this methodology. In this review we attempt at analyzing the causes of this variable behavior and at providing hints to increase the chances of experimental success.

PMID: 25797005 [PubMed - in process]

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins Publication date: April 2015 Source:Journal of Magnetic Resonance, Volume 253</br> Author(s): Enrico Ravera , Tobias Schubeis , Tommaso Martelli , Marco Fragai , Giacomo Parigi , Claudio Luchinat</br> Resolution and sensitivity in solid state NMR (SSNMR) can rival the results achieved by solution NMR, and even outperform them in the case of large systems. However, several factors affect the spectral quality in SSNMR samples, and not all systems turn out to be equally...	nmrlearner	Journal club	0	03-20-2015 01:48 AM
[NMR paper] Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation. Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation. Related Articles Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation. J Magn Reson. 2014 Sep 20;248C:8-12 Authors: Krushelnitsky A, Zinkevich T, Reif B, Saalwächter K Abstract (15)N NMR relaxation rate R1? measurements reveal that a substantial fraction of residues in the microcrystalline chicken alpha-spectrin SH3 domain protein undergoes dynamics in the ?s-ms...	nmrlearner	Journal club	0	10-06-2014 12:37 PM
[NMR paper] Slow motions in microcrystalline proteins as observed by MAS-dependent 15N rotating-frame NMR relaxation Slow motions in microcrystalline proteins as observed by MAS-dependent 15N rotating-frame NMR relaxation Publication date: Available online 20 September 2014 Source:Journal of Magnetic Resonance</br> Author(s): Alexey Krushelnitsky , Tatiana Zinkevich , Bernd Reif , Kay Saalwächter</br> 15N NMR relaxation rate R 1? measurements reveal that a substantial fraction of residues in the microcrystalline chicken alpha-spectrin SH3 domain protein undergoes dynamics in the ?s - ms timescale range. On the basis of a comparison of 2D site-resolved with 1D integrated 15N...	nmrlearner	Journal club	0	09-20-2014 07:51 PM
Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins Abstract Relaxation parameters such as longitudinal relaxation are susceptible to artifacts such as spin diffusion, and can be affected by paramagnetic impurities as e.g. oxygen, which make a quantitative interpretation difficult. We present here the site-specific measurement of 13C and 15N heteronuclear rates in an immobilized protein. For methyls, a strong effect is expected due to the three-fold rotation of the methyl group. Quantification of the 13C...	nmrlearner	Journal club	0	07-03-2014 06:04 AM
[NMR paper] Drug screening strategy for human membrane proteins: from NMR protein backbone structure to in silica- and NMR-screened hits. Drug screening strategy for human membrane proteins: from NMR protein backbone structure to in silica- and NMR-screened hits. Related Articles Drug screening strategy for human membrane proteins: from NMR protein backbone structure to in silica- and NMR-screened hits. Biochem Biophys Res Commun. 2014 Feb 10; Authors: Lindert S, Maslennikov I, Chiu E, Pierce LC, Andrew McCammon J, Choe S Abstract About 8,000 genes encode membrane proteins in the human genome. The information about their druggability will be very useful to facilitate...	nmrlearner	Journal club	0	02-15-2014 08:52 PM
Drug screening strategy for human membrane proteins: from NMR protein backbone structure to in silica- and NMR-screened hits Drug screening strategy for human membrane proteins: from NMR protein backbone structure to in silica- and NMR-screened hits Publication date: Available online 10 February 2014 Source:Biochemical and Biophysical Research Communications</br> Author(s): Steffen Lindert , Innokentiy Maslennikov , Ellis Chiu , Levi C Pierce , J. Andrew McCammon , Senyon Choe</br> About 8,000 genes encode membrane proteins in the human genome. The information about their druggability will be very useful to facilitate drug discovery and development. The main problem, however,...	nmrlearner	Journal club	0	02-10-2014 08:46 PM
Solid-state NMR of proteins sedimented by ultracentrifugation [Chemistry] Solid-state NMR of proteins sedimented by ultracentrifugation Bertini, I., Luchinat, C., Parigi, G., Ravera, E., Reif, B., Turano, P.... Date: 2011-06-28 Relatively large proteins in solution, spun in NMR rotors for solid samples at typical ultracentrifugation speeds, sediment at the rotor wall. The sedimented proteins provide high-quality solid-state-like NMR spectra suitable for structural investigation. The proteins fully revert to the native solution state when spinning is stopped, allowing one to study them in both conditions. Transiently sedimented proteins can be considered a...	nmrlearner	Journal club	0	06-29-2011 04:45 AM
Solid-state NMR of proteins sedimented by ultracentrifugation. Solid-state NMR of proteins sedimented by ultracentrifugation. Solid-state NMR of proteins sedimented by ultracentrifugation. Proc Natl Acad Sci U S A. 2011 Jun 13; Authors: Bertini I, Luchinat C, Parigi G, Ravera E, Reif B, Turano P Relatively large proteins in solution, spun in NMR rotors for solid samples at typical ultracentrifugation speeds, sediment at the rotor wall. The sedimented proteins provide high-quality solid-state-like NMR spectra suitable for structural investigation. The proteins fully revert to the native solution state when...	nmrlearner	Journal club	0	06-15-2011 01:15 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