Structure in solution of the major cold-shock protein from Bacillus subtilis
β Scribed by Schnuchel, A.; Wiltscheck, R.; Czisch, M.; Herrler, M.; G. Wllllmsky, ; Graumann, P.; Marahiel, M. A.; Holak, T. A.
- Book ID
- 109784621
- Publisher
- Nature Publishing Group
- Year
- 1993
- Tongue
- English
- Weight
- 611 KB
- Volume
- 364
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/364169a0
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## Abstract The solution structure of the __Bacillus subtilis__ protein YndB has been solved using NMR to investigate proposed biological functions. The YndB structure exhibits the helixβgrip fold, which consists of a Ξ²βsheet with two small and one long Ξ±βhelix, forming a hydrophobic cavity that pr
In the cold-shock protein CspB from Bacillus subtilis three exposed Phe residues (F15, F17, and F27) are essential for its function in binding to single-stranded nucleic acids. Usually, the hydrophobic Phe side chains are buried in folded proteins. We asked here whether the exposition of the essenti