A stable single-layer β-sheet without a hydrophoe
- 1 February 1998
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 5 (2) , 115-119
- https://doi.org/10.1038/nsb0298-115
Abstract
Outer surface protein A from the Lyme disease spirochete Borrelia burgdorferi contains a single-layer beta-sheet connecting the N- and C-terminal globular domains. The central beta-sheet consists largely of polar amino acids and is solvent-exposed on both faces, which so far appears to be unique among known protein structures. We show that the single-layer beta-sheet segment is surprisingly stable (deltaG for hydrogen exchange is approximately 8 kcal mol(-1) at 45 degrees C). Possible factors contributing to the stability of the single-layer beta-sheet are discussed based on an analysis of the crystal structure.Keywords
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