## Abstract Redox proteins participate in many metabolic routes, in particular those related to energy conversion. Proteinβprotein complexes of redox proteins are characterized by a weak affinity and a short lifetime. Twoβdimensional NMR spectroscopy has been applied to many redox protein complexes
NMR studies of structure and dynamics of isotope enriched proteins
β Scribed by Gerhard Wagner; V. Thanabal; Brian J. Stockman; Jeffrey W. Peng; N. R. Nirmala; Sven G. Hyberts; Matthew S. Goldberg; David J. Detlefsen; Robert T. Clubb; Marc Adler
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1992
- Tongue
- English
- Weight
- 585 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0006-3525
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The solution structure of polypeptides can now be achieved through NMR spectroscopy, as long as the molecular mass does not much exceed 40 000 Da [1][2][3][4][5]. The determination of the structure of heme proteins, however, requires the knowledge of the position of the iron and of the atoms of the
The IR phonon spectra of 10 B, 11 B, and 13 C isotope-enriched boron carbide with the compositions B 4.3 C, B 6.5 C, and B 10 C are presented. Speci5c phonons are attributed to the stretching and the bending mode of a small concentration of CCC chains, whose occurrence seems to depend on the speci5c