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- URN zum Zitieren dieses Dokuments:
- urn:nbn:de:bvb:355-epub-462710
- DOI zum Zitieren dieses Dokuments:
- 10.5283/epub.46271
Zusammenfassung
A choline-binding module from pneumococcal LytA autolysin, LytA(239-252,) was reported to have a highly stable nativelike beta-hairpin in aqueous solution, which turns into a stable amphipathic alpha-helix in the presence of micelles. Here, we aim to obtain insights into this DPC-micelle triggered beta-hairpin-to-alpha-helix conformational transition using photo-CIDNP NMR experiments. Our results ...
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