ISSN:
1573-5001
Keywords:
Interleukin-1β
;
Interleukin-1 receptor antagonist protein
;
Protein NMR spectroscopy
;
Secondary chemical shift
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Summary 1Hα,13Cα, and15Nα secondary chemical shifts, defined as the difference between the observed value and the random coil value, have been calculated for interleukin-1 receptor antagonist protein and interleukin-1β. Averaging of the secondary chemical shifts with those of adjacent residues was used to smooth out local effects and to obtain a correlation dependent on secondary structure. Differences and similarities in the placement of secondary structure elements in the primary segdences of these structurally homologous proteins are manifested in the smoothed secondary chemical shifts of all three types of nuclei. The close correlation observed between the secondary chemical shifts and the previously defined locations of secondary structure, as defined by traditional methods, exemplifies the advantage of chemical shifts to delineate regions of secondary structure.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02192848
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