Author

U. Eckhard

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:protein design· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

A. Gogoll· 1 shared A. Moyer· 1 shared A. Söderholm· 1 shared C. H. Arrowsmith· 1 shared D. Andersson· 1 shared D. Baker· 1 shared E. Marcos· 1 shared F. X. Gomis-Rüth· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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1 shared paperBiochemistry

A. Gogoll

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2 papers

Recent·Most cited

De Novo Design of Immunoglobulin-like Domains

T. M. Chidyausiku, S. R. Mendes, J. C. Klima, U. Eckhard, S. Houliston, M. Nadal, J. Roel-Touris, T. Guevara, H. K. Haddox, A. Moyer, C. H. Arrowsmith, F. X. Gomis-Rüth, D. Baker, E. Marcos

This paper introduces design rules for immunoglobulin-like domains and demonstrates the de novo creation of stable, functional scaffolds with improved biophysical properties.

bioRxiv · Dec 20, 2021 · PreprintBiochemistry

Structure and mechanism of a phage-encoded SAM lyase revises catalytic function of enzyme family

X. Guo, A. Söderholm, S. Kanchugal P, G. V. Isaksen, O. Warsi, U. Eckhard, S. Trigüis, A. Gogoll, J. Jerlström-Hultqvist, J. Aqvist, D. Andersson, M. Selmer

The paper reveals the structure and mechanism of phage-encoded SAM lyases, showing they function as lyases rather than hydrolases, forming MTA and L-homoserine lactone through a unimolecular reaction.

bioRxiv · Aug 16, 2020Biochemistry