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A de novo peptide hexamer with a mutable channel

DOI: 10.1038/nchembio.692 DOI Help
PMID: 22037471 PMID Help

Authors: Nathan Zaccai (University of Bristol) , Bertie Chi (University of Bristol) , Andrew Thomson (University of Bristol) , Aimee L Boyle (University of Bristol) , Gail J Bartlett (University of Bristol) , Marc Bruning (University of Bristol) , Noah Linden (University of Bristol) , Richard B Sessions (University of Bristol) , Paula J Booth (University of Bristol) , Leo Brady (University of Bristol) , Derek N Woolfson (University of Bristol)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Chemical Biology , VOL 7 (12) , PAGES 935 - 941

State: Published (Approved)
Published: October 2011
Diamond Proposal Number(s): 7131

Open Access Open Access

Abstract: The design of new proteins that expand the repertoire of natural protein structures represents a formidable challenge. Success in this area would increase understanding of protein structure and present new scaffolds that could be exploited in biotechnology and synthetic biology. Here we describe the design, characterization and X-ray crystal structure of a new coiled-coil protein. The de novo sequence forms a stand-alone, parallel, six-helix bundle with a channel running through it. Although lined exclusively by hydrophobic leucine and isoleucine side chains, the 6-Å channel is permeable to water. One layer of leucine residues within the channel is mutable, accepting polar aspartic acid and histidine side chains, which leads to subdivision and organization of solvent within the lumen. Moreover, these mutants can be combined to form a stable and unique (Asp-His)3 heterohexamer. These new structures provide a basis for engineering de novo proteins with new functions

Journal Keywords: Crystallography; X-Ray; Histidine; Models; Molecular; Oligopeptides; Protein; Synthetic Biology

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I02-Macromolecular Crystallography , I04-Macromolecular Crystallography

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