Quantitative characterization of all single amino acid variants of a viral capsid-based drug delivery vehicle

Emily C. Hartman; Christopher M. Jakobson; Andrew H. Favor; Marco J. Lobba; Ester Álvarez-Benedicto; Matthew B. Francis; Danielle Tullman-Ercek

doi:10.1038/s41467-018-03783-y

Nature Communications (Apr 2018)

Quantitative characterization of all single amino acid variants of a viral capsid-based drug delivery vehicle

Emily C. Hartman,
Christopher M. Jakobson,
Andrew H. Favor,
Marco J. Lobba,
Ester Álvarez-Benedicto,
Matthew B. Francis,
Danielle Tullman-Ercek

Affiliations

Emily C. Hartman: Department of Chemistry, University of California
Christopher M. Jakobson: Department of Chemical and Biomolecular Engineering, University of California
Andrew H. Favor: Department of Chemistry, University of California
Marco J. Lobba: Department of Chemistry, University of California
Ester Álvarez-Benedicto: Department of Chemistry, University of California
Matthew B. Francis: Department of Chemistry, University of California
Danielle Tullman-Ercek: Department of Chemical and Biological Engineering, Northwestern University

DOI: https://doi.org/10.1038/s41467-018-03783-y
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 11

Abstract

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Self-assembling proteins have important applications in industrial technologies, but it is difficult to predict how mutations affect assembly. Here the authors present SyMAPS, coupling comprehensive codon mutagenesis with high-throughput sequencing, and apply it to bacteriophage capsid protein.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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