Determination of 13C? relaxation times in uniformly 13C/15N-enriched proteins

1995 ◽  
Vol 5 (2) ◽  
Author(s):  
Jan Engelke ◽  
Heinz R�terjans
1981 ◽  
Vol 78 (1) ◽  
pp. 227-236 ◽  
Author(s):  
S. Ochiai ◽  
K. Iimura ◽  
M. Takeda ◽  
M. Ohuchi ◽  
K. Matsushita

1987 ◽  
Vol 52 (2) ◽  
pp. 541-546 ◽  
Author(s):  
Vladimír Mlynárik

Carbon-13 relaxation times in the rotating frame were used to study the exchange between unequally populated rotamers of 2-furaldehyde. Calculated free activation energy and activation enthalpy are in good agreement with the results of 1H line shape analysis. Accuracy and reliability of this method in comparison with the line shape analysis is discussed.


1982 ◽  
Vol 201 (3) ◽  
pp. 605-613 ◽  
Author(s):  
D Kaplan ◽  
G Navon

The conformation of bilirubin and its dimethyl ester in dimethyl sulphoxide (DMSO) was investigated by n.m.r. spectroscopy. The chemical shifts of the pyrrole NH and Lactam protons of bilirubin and its dimethyl ester in DMSO indicate a strong interaction with the solvent. Inter-proton distances were calculated from nuclear Overhauser effects (NOE), selective and non-selective relaxation times (T1) and rotational correlation times taken from 13C relaxation times. The interproton distances indicate that the conformation of the skeleton of bilirubin and its dimethyl ester in DMSO is similar to that of bilirubin and mesobilirubin in the crystalline state and in chloroform solutions, except for a possible slight twist of the pyrrolenone rings about the methine bonds, which may be a consequence of solvation of the NH groups by DMSO. Unlike in chloroform solutions, no direct hydrogen-bonding occurs between the carboxylic acid and the lactam groups of bilirubin in DMSO, as shown by the absence of an NOE between these groups. The fast exchange of the pyrrole NH protons with 2H shows that no hydrogen-bonding occurs between these protons and the propionic residues, in line with their solvation by DMSO. From the above results, and from the slowness of the internal motion of the propionic residues of bilirubin and its dimethyl ester, it is concluded that these residues are tied to the skeleton via bound solvent molecules.


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