| Abstrakt: |
The secondary structure of BSPI-2 has been determined using information obtained exclusively fromH-NMR recordings of Nuclear Overhauser effects, coupling constants and hydrogen exchange rates. It is shown that the protein contains one α-helix and a six-stranded β-sheet. Four of the strands form an anti-parallel β-sheet, and two form a parallel. In addition, six turns and one half turn have been identified. The segment containing the active site shows no secondary structure. This secondary structure is in close agreement with the structure determined by X-ray crystallography ( C.A. McPhalen and M.N.G. James, Biochemistry 26, 261-269 (1987)) and from NMR by means of distance geometry followed by restrained molecular dynamics based on the total number of NOE effects ( G.M. Clore, A.M. Gronenborn, M. Kj/er and F.M. Poulsen, Protein Engineering 1, 305-311 (1987)). [ABSTRACT FROM AUTHOR] |
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