Archive for November 18, 2014

A.S. Mazur has presented a lecture

On November 18th A.S. Mazur (CMR specialist) has presented a lecture titled “Magnetic phase inhomogeneity in manganates (55Mn NMR study)”

Dalton Trans. 2014

T.B. Anisimova, M. Fátima C. Guedes da Silva, V.Yu. Kukushkin, A.J. L. Pombeiro, K.V. Luzyanin

“Metal-mediated coupling of amino acid esters with isocyanides leading to new chiral acyclic aminocarbene complexes”

Dalton Trans., 2014, 43, 15861-15871

DOI: 10.1039/c4dt01917b

Metal-mediated coupling between equimolar amounts of cis-[PdCl2(CNR1)2] (1–5) and the amino acid esters L-HTyrOMe (7) or L-HProOtBu (8) proceeds at 40 °C in chloroform over ca. 6 h. The subsequent workup affords the complexes cis-[PdCl2(CNR1){C(TyrOMe)[double bond, length as m-dash]NHR1}] (R1 = Xyl 9, 2-Cl-6-Me-C6H310) or cis-[PdCl2(CNR1){C(ProOtBu)[double bond, length as m-dash]NHR1}] (R1 = Xyl 11, 2-Cl-6-Me-C6H312, Cy 13, tBu 14, 2-naphthyl 15) in good to excellent isolated yields (75–94%). The corresponding reaction between trans-[PdI2(CNR1)2] (6) and 8 brings about the formation of trans-[PdI2(CNCy){C(ProOtBu)[double bond, length as m-dash]NHCy}] (16, 76% isolated yield). The reaction of 6 with 7 proceeds non-selectively giving a broad mixture of products. Complexes 9–16 were characterized by elemental analyses (C, H, N), ESI+/−-MS, IR, 1D (1H, 13C{H}) and 2D (1H,1H-COSY, 1H,13C-HMQC/1H,13C-HSQC, 1H,13C-HMBC) NMR spectroscopic techniques, and by single-crystal X-ray diffraction (for 9, 11–13, and 16).

Excursion for 2nd year students

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2nd year students of the Department of Chemistry have visited the Center and learned about the NMR and EPR spectrometers.


V.V. Kachala, NMR of liquids lessons

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From 10th to 14th of November specialist from Bruker company V.V. Kachala conducts a series of lessons on NMR spectrometers for new employees of the Center.

Sevastian Rabdano has presented a lecture

On November 6th Sevastian Rabdano (member of Prof. Skrynnikov’s laboratory of bio-NMR) has presented a lecture titled “RNA-recognizing RRM2 domain of TDP-43 protein: oxidative stress leads to changes in conformation, proteolysis, formation of inclusion bodies and neurodegenerative deceases”.


Total in october 1465 service applications were carried out.

All together measured:

  • 1422 1H spectra
  • 347 13C spectra
  • 220 DEPT spectra
  • 15 COSY spectra
  • 31 NOESY spectra
  • 51 31P spectra
  • 150 19F spectra

127 applications were carried out which jointly took 3036 hours of measurements.