Watching protein structure at work in living cells using NMR spectroscopy

		BioNMR > Educational resources > Journal club
Watching protein structure at work in living cells using 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

02-03-2013, 10:13 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,778

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

Watching protein structure at work in living cells using NMR spectroscopy

Watching protein structure at work in living cells using NMR spectroscopy

December 2012
Publication year: 2012
Source:Current Opinion in Chemical Biology, Volume 16, Issues 5–6

Isotope-assisted multi-dimensional NMR spectroscopy can now be applied to proteins inside living cells. The technique, called in-cell NMR, aims to investigate the structures, interactions and dynamics of proteins under their native conditions, ideally at an atomic resolution. The application has begun with bacterial cells but has now expanded to mammalian cultured cells, such as HeLa cells. The importance of the realization of such ‘in-mammalian cell’ NMR should be stressed, as these are the cells most often employed in cell biology. Hence, a substantially wide range of application would be possible in the near future once the technique has been well developed.
Highlights

? Advances in in-cell NMR spectroscopy of biomacromolecules. ? Escherichia coli, yeasts, Xenopus laevis oocytes and mammalian cell lines can be used. ? Structures, dynamics and interactions of proteins in living cells are studied. ? Proteins in the intracellular space behave differently from those in vitro.

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Protein dynamics in living cells studied by in-cell NMR spectroscopy Protein dynamics in living cells studied by in-cell NMR spectroscopy Available online 11 January 2013 Publication year: 2013 Source:FEBS Letters</br> </br> Most proteins function in cells where protein concentrations can reach 400g/l. However, most quantitative studies of protein properties are performed in idealized, dilute conditions. Recently developed in-cell NMR techniques can provide protein structure and other biophysical properties inside living cells at atomic resolution. Here we review how protein dynamics, including global and internal motions have been...	nmrlearner	Journal club	0	02-03-2013 10:13 AM
High-Resolution HeteronuclearMultidimensional NMRof Proteins in Living Insect Cells Using a Baculovirus Protein ExpressionSystem High-Resolution HeteronuclearMultidimensional NMRof Proteins in Living Insect Cells Using a Baculovirus Protein ExpressionSystem Jumpei Hamatsu, Daniel O’Donovan, Takashi Tanaka, Takahiro Shirai, Yuichiro Hourai, Tsutomu Mikawa, Teppei Ikeya, Masaki Mishima, Wayne Boucher, Brian O. Smith, Ernest D. Laue, Masahiro Shirakawa and Yutaka Ito http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja310928u/aop/images/medium/ja-2012-10928u_0005.gif Journal of the American Chemical Society DOI: 10.1021/ja310928u...	nmrlearner	Journal club	0	01-27-2013 11:41 PM
On-Cell MAS NMR: PhysiologicalClues from Living Cells On-Cell MAS NMR: PhysiologicalClues from Living Cells Giorgia Zandomeneghi, Karin Ilg, Markus Aebi and Beat H. Meier http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja307467p/aop/images/medium/ja-2012-07467p_0007.gif Journal of the American Chemical Society DOI: 10.1021/ja307467p http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/PBl2HVolQkY	nmrlearner	Journal club	0	10-15-2012 10:49 PM
STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells. STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells. STD and trNOESY NMR study of receptor-ligand interactions in living cancer cells. Chembiochem. 2011 Mar 21;12(5):695-9 Authors: Potenza D, Vasile F, Belvisi L, Civera M, Araldi EM	nmrlearner	Journal club	0	07-19-2011 07:52 PM
13C direct-detection biomolecular NMR spectroscopy in living cells. 13C direct-detection biomolecular NMR spectroscopy in living cells. 13C direct-detection biomolecular NMR spectroscopy in living cells. Angew Chem Int Ed Engl. 2011 Mar 1;50(10):2339-41 Authors: Bertini I, Felli IC, Gonnelli L, Kumar M V V, Pierattelli R	nmrlearner	Journal club	0	06-18-2011 01:10 PM
[NMR paper] Multidimensional NMR spectroscopy for protein characterization and assignment inside cells. Multidimensional NMR spectroscopy for protein characterization and assignment inside cells. Related Articles Multidimensional NMR spectroscopy for protein characterization and assignment inside cells. J Am Chem Soc. 2005 Aug 10;127(31):10848-9 Authors: Reardon PN, Spicer LD High-field, heteronuclear NMR spectroscopy of biological macromolecules in native cellular environments is limited by the low concentrations present and the long data acquisition times needed for the experiments. Successful 1D and 2D heteronuclear NMR data have been...	nmrlearner	Journal club	0	12-01-2010 06:56 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