Proton, carbon, and nitrogen chemical shifts accurately delineate differences and similarities in secondary structure between the homologous proteins IRAP and IL-1 beta
| Autor: | David P. Brunner, Nancy A. Strakalaitis, Martin R. Deibel, Terrence A. Scahill, Anthony W. Yem, Brian J. Stockman |
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| Rok vydání: | 1992 |
| Předmět: |
Magnetic Resonance Spectroscopy
Proton Sequence Homology Amino Acid Stereochemistry Nitrogen Chemical shift Sialoglycoproteins Protein NMR Spectroscopy Molecular Sequence Data chemistry.chemical_element Protein superfamily Biochemistry Random coil Carbon Protein Structure Secondary Interleukin 1 Receptor Antagonist Protein chemistry Biophysics Amino Acid Sequence Protons Protein secondary structure Spectroscopy Interleukin-1 |
| Zdroj: | Journal of biomolecular NMR. 2(6) |
| ISSN: | 0925-2738 |
| Popis: | 1H alpha, 13C alpha, and 15N alpha secondary 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-1 beta. 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 sequences 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. |
| Databáze: | OpenAIRE |
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