A 1H-NMR study of the solution conformation of secretin resonance assignment and secondary structure
β Scribed by Angela M. Gronenborn; Gunter Bovermann; G.Marius Clore
- Book ID
- 115918992
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 340 KB
- Volume
- 215
- Category
- Article
- ISSN
- 0014-5793
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π SIMILAR VOLUMES
Sequence-specific ~H and ~SN resonance assignments have been made for 137 of the 146 nonprolyl residues in oxidized Desulfovibrio desulfuricans [Essex 6] flavodoxin. Assignments were obtained by a concerted analysis of the heteronuclear three-dimensional ~H-~SN NOESY-HMQC and TOCSY-HMQC data sets, r
## Abstract The solution conformation of Ξ²βcasein phosphopeptide (CPP) was studied by ^1^H NMR spectroscopy. As a prerequisite to the conformational analysis the spectral assignment was carried out for CPP in the Ca^2+^βfree and βbound states by the use of twoβdimensional NMR spectroscopy. The assi