-transparent.png){kind=logo}
The secondary structure of crambin in solution has been determined using two-dimensional NMR and is found to be essentially identical to that of the crystal structure. The H-D exchange of most amide protons can be accounted for in terms of the hydrogen bonds found in the X-ray structure. Exceptions are the amide protons of Cys-4 and Ser-6, which exchange more slowly than expected, and of Asn-46 for which the exchange is faster. These results might be explained by a slightly different conformation of the C-terminal region of the protein in solution. The slow exchange of the amides of Cys-32 and Glu-23 might be due to aggregation involving an extremely hydrophobic part of the protein in solution.
R M Lamerichs, and
L J Berliner, and
R Boelens, and
A De Marco, and
M Llinàs, and
R Kaptein
November 1990,
European journal of biochemistry,
R M Lamerichs, and
L J Berliner, and
R Boelens, and
A De Marco, and
M Llinàs, and
R Kaptein
December 1995,
Biochemical and biophysical research communications,
R M Lamerichs, and
L J Berliner, and
R Boelens, and
A De Marco, and
M Llinàs, and
R Kaptein
February 2014,
Progress in nuclear magnetic resonance spectroscopy,
R M Lamerichs, and
L J Berliner, and
R Boelens, and
A De Marco, and
M Llinàs, and
R Kaptein
November 1996,
Solid state nuclear magnetic resonance,
R M Lamerichs, and
L J Berliner, and
R Boelens, and
A De Marco, and
M Llinàs, and
R Kaptein
May 1991,
Biochemistry,
R M Lamerichs, and
L J Berliner, and
R Boelens, and
A De Marco, and
M Llinàs, and
R Kaptein
May 1995,
International journal of peptide and protein research,
R M Lamerichs, and
L J Berliner, and
R Boelens, and
A De Marco, and
M Llinàs, and
R Kaptein
December 1995,
International journal of peptide and protein research,
R M Lamerichs, and
L J Berliner, and
R Boelens, and
A De Marco, and
M Llinàs, and
R Kaptein
April 1987,
Biochemical and biophysical research communications,
R M Lamerichs, and
L J Berliner, and
R Boelens, and
A De Marco, and
M Llinàs, and
R Kaptein
January 1995,
Acta crystallographica. Section D, Biological crystallography,
R M Lamerichs, and
L J Berliner, and
R Boelens, and
A De Marco, and
M Llinàs, and
R Kaptein
December 2010,
Journal of the American Chemical Society,
