Orientation of the Chemical Shielding Anisotropy Tensor of the Carbonate Carbon in Diphenyl Carbonate and Its Consequences for NMR Studies on Polycarbonate

1998 ◽  
Vol 31 (17) ◽  
pp. 5818-5822 ◽  
Author(s):  
P. Robyr ◽  
M. Utz ◽  
Z. Gan ◽  
C. Scheurer ◽  
M. Tomaselli ◽  
...  
1982 ◽  
Vol 60 (16) ◽  
pp. 2113-2117 ◽  
Author(s):  
Roderick E. Wasylishen ◽  
Robert E. Lenkinski ◽  
Charles Rodger

Mercury-199 spin-lattice relaxation times are reported for several mercury(II) compounds at 5.875 and 9.40 T. From the field dependence of T1, in Hg(CN)2, Hg(CH3)2, and Hg(C6H5)2, 199Hg chemical shielding anisotropies of 3800, 5820, and 5800 ppm are calculated. The errors in these of estimates of Δσ are at least 10%. Some implications of the large Δσ(199Hg) values in high field nmr studies are discussed.


1999 ◽  
Vol 96 (9/10) ◽  
pp. 1580-1584 ◽  
Author(s):  
I. Ségalas ◽  
S. Desjardins ◽  
H. Oulyadi ◽  
Y. Prigent ◽  
S. Tribouillard ◽  
...  

1994 ◽  
Vol 91 ◽  
pp. 697-703 ◽  
Author(s):  
B Gillet ◽  
BT Doan ◽  
C Verre-Sebrie ◽  
O Fedeli ◽  
JC Beloeil ◽  
...  

1980 ◽  
Vol 41 (C8) ◽  
pp. C8-32-C8-35
Author(s):  
Y. Nakamura ◽  
M. Niibe ◽  
M. Shimoji
Keyword(s):  

1988 ◽  
Vol 49 (C8) ◽  
pp. C8-1713-C8-1714
Author(s):  
K. Le Dang ◽  
P. Veillet ◽  
H. Sakakima ◽  
R. Krishnan
Keyword(s):  

1990 ◽  
Vol 63 (03) ◽  
pp. 499-504 ◽  
Author(s):  
A Electricwala ◽  
L Irons ◽  
R Wait ◽  
R J G Carr ◽  
R J Ling ◽  
...  

SummaryPhysico-chemical properties of recombinant desulphatohirudin expressed in yeast (CIBA GEIGY code No. CGP 39393) were reinvestigated. As previously reported for natural hirudin, the recombinant molecule exhibited abnormal behaviour by gel filtration with an apparent molecular weight greater than that based on the primary structure. However, molecular weight estimation by SDS gel electrophoresis, FAB-mass spectrometry and Photon Correlation Spectroscopy were in agreement with the theoretical molecular weight, with little suggestion of dimer or aggregate formation. Circular dichroism studies of the recombinant molecule show similar spectra at different pH values but are markedly different from that reported by Konno et al. (13) for a natural hirudin-variant. Our CD studies indicate the presence of about 60% beta sheet and the absence of alpha helix in the secondary structure of recombinant hirudin, in agreement with the conformation determined by NMR studies (17)


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