Details

Autor(en) / Beteiligte

• D'Souza, Areetha
• Wu, Xiangyang
• Yeow, Edwin Kok Lee
• Bhattacharjya, Surajit

Titel

Designed Heme-Cage [beta]-Sheet Miniproteins

Ist Teil von

• Angewandte Chemie International Edition, 2017-05, Vol.56 (21), p.5904

Auflage

International ed. in English

Ort / Verlag

Weinheim: Wiley Subscription Services, Inc

Erscheinungsjahr

2017

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• The structure and function of naturally occurring proteins are governed by a large number of amino acids (≥100). The design of miniature proteins with desired structures and functions not only substantiates our knowledge about proteins but can also contribute to the development of novel applications. Excellent progress has been made towards the design of helical proteins with diverse functions. However, the development of functional [beta]-sheet proteins remains challenging. Herein, we describe the construction and characterization of four-stranded [beta]-sheet miniproteins made up of about 19 amino acids that bind heme inside a hydrophobic binding pocket or "heme cage" by bis-histidine coordination in an aqueous environment. The designed miniproteins bound to heme with high affinity comparable to that of native heme proteins. Atomic-resolution structures confirmed the presence of a four-stranded [beta]-sheet fold. The heme-protein complexes also exhibited high stability against thermal and chaotrope-induced unfolding.