IBS Grenoble

grenobleibs

Resp. This email address is being protected from spambots. You need JavaScript enabled to view it. (This email address is being protected from spambots. You need JavaScript enabled to view it.)

Corr. This email address is being protected from spambots. You need JavaScript enabled to view it. (This email address is being protected from spambots. You need JavaScript enabled to view it. tel : ...)

IBS NMR Platform

 

Panorama 3 RMN-small 16965Technical description of the platform

TGIR Spectrometer:
+ 950SB [Liquid,Solid]

Bruker Avance II HD 950 MHz Spectrometer equiped with TXI cryosonde (S/B =x) working from 4°C to 50 °C,
with a solid equipement including a 3.2 mm solid sonde ( 1H, 13C, 15N/ 31P) (?r < 20 kHz)
and 1,3 mm ( ?r < 80 kHz) ( 1H, 13C, 15N / 31P)

950 MHz with sample changer

Liquid sondes :
- Cryo TCI (1H, 13C, 15N, 2H), 5 mm, z-gradients (0°<T
Solid sondes:
- MAS (1H, 13C, 15N), 3,2 mm, E-free (?r < 25 kHz)
- MAS (1H, 13C, 15N), 1,3 mm, +lock( ?r < 60 kHz)

grenoble-brukerAvailable RMN experiences :

Fast-NMR (Best, sofast ...), real-time nmr with injector, liquid Bio-NMR (simple, double and triple resonances), dipolar relaxation and dispersion  relaxation, methyls nmr, ...

 

Main areas of application :

Structures of macromolecules, kinetic measurement, protein folding measurement, relaxation dispertio

 

Other NMR equipements at the IBS (Ralf-NMR, Bio-NMR):

850 MHz Bruker Avance III HD with sample changer

Liquid sondes:
- Cryo TCI (1H, 13C, 15N, 2H), 5 mm, z-gradients
- Cryo TCI (1H, 13C, 15N, 2H), 1,7 mm , z-gradients

700 MHz Bruker Avance III HD Liquid / Solid

Liquid sondes:
- Cryo QCI (1H/31P, 13C, 15N, 2H), 5 mm, z-gradients
Solid sondes:
- MAS (1H, 13C, 15N), 3,2 mm, E-free
- MAS (1H, 13C, 15N), 1,3 mm, +lock

600 MHz (Bruker-1) Bruker Avance III HD Liquid

Liquid sondes:
- Cryo TCI (1H, 13C, 15N, 2H), 5 mm, x,y,z-gradients

600 MHz (Bruker-2) Bruker Avance III HD Liquid / Solid

Liquid sondes:
- QCI (1H/19F, 13C, 15N, 2H), 5 mm, z-gradients
Solid sondes:
- MAS (1H, 13C, 15N), 3,2 mm
- MAS (1H, 13C, 15N, 31P), 1,3 mm, +lock

 

Liquid / Solid 600 MHz (Agilent) Agilent vnmrs

Liquid sondes:
- penta (1H/31P, 13C, 15N, 2H), 5 mm, z-gradients
Solide sondes:
- MAS (1H, 13C, 15N), 3,2 mm
- MAS (1H, 13C, 15N), 1,6 mm, +lock, +z-gradients

 

About IBS

Both research center, technical facilities, reception site and scientific training, the Institute of Structural Biology (IBS) is dedicated to the development of research in structural biology, a field of research which is crucial for the understanding of the fundamental biological mechanisms. IBS is part of a larger ensemble, the Partnership for Structural Biology (PSB), whose primary objective is the study of proteins with medical interest.

 

Going to IBS :

 

JavaScript must be enabled in order for you to use Google Maps.
However, it seems JavaScript is either disabled or not supported by your browser.
To view Google Maps, enable JavaScript by changing your browser options, and then try again.

 

 How to come

Some recent publications:

  • The RNA-binding region of human TRBP interacts with microRNA precursors through two independent domains.
    Benoit MP, Imbert L, Palencia A, Pérard J, Ebel C, Boisbouvier J, Plevin MJ.
    Nucleic Acids Res. 2013 ;41(7):4241-52. link
  • Interaction of non-structural protein 5A of hepatitis C virus with SH3 domains using non-canonical binding sites.
    Schwarten M, Solyom Z, Feuerstein SE, Aladag A, Hoffmann S, Willbold D, Brutscher B.
    Biochemistry. 2013 Aug 15. [Epub ahead of print] link
  • Structure of Enterococcus faeciuml,d-Transpeptidase Acylated by Ertapenem Provides Insight into the Inactivation Mechanism.
    Lecoq L, Dubée V, Triboulet S, Bougault C, Hugonnet JE, Arthur M, Simorre JP.
    ACS Chem Biol. 2013 Apr 12. [Epub ahead of print] link
  • Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate.
    Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B.
    J Am Chem Soc. 2012 May 16;134(19):8066-9. link.
  • Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy.
    Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P.
    J Am Chem Soc. 2012 Sep 12;134(36):14800-7. link.
  • Plevin, M. J., D. L. Bryce, and J. Boisbouvier. 
    Direct detection of ch/pi interactions in proteins. 
    Nature Chemistry (2010) 2, no. 6: 466-471. link.
  • Second double-stranded RNA binding domain of dicer-like ribonuclease 1: structural and biochemical characterization.
    Burdisso P, Suarez IP, Bologna NG, Palatnik JF, Bersch B, Rasia RM.
    Biochemistry. 2012 Dec 21;51(51):10159-66. link.
  • Dynamics induced by ?-lactam antibiotics in the active site of Bacillus subtilis L,D-transpeptidase.
    Lecoq L, Bougault C, Hugonnet JE, Veckerlé C, Pessey O, Arthur M, Simorre JP.
    Structure. 2012 May 9;20(5):850-61. link.