Author

L. Staby

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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Biophysics· 2

Signature Assays, Organisms & Methods

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Assay:protein structure· 2 Approach:deep learning· 1 Approach:experimental assay· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

B. B. Kragelund· 2 shared A. D. Due· 1 shared A. Escobedo· 1 shared A. Sottini· 1 shared B. Schuler· 1 shared B. Topal· 1 shared C. B. Fernandes· 1 shared C. R. O. Bartling· 1 shared

Activity by Year

2022-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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2 shared papersBiophysics

B. B. Kragelund

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2 papers

Recent·Most cited

The importance of stereochemistry in the disorder-order continuum of protein-protein interactions

E. A. Newcombe, A. D. Due, A. Sottini, C. B. Fernandes, L. Staby, E. Delaforge, C. R. O. Bartling, I. Brakti, K. Bugge, B. Schuler, K. Skriver, J. G. Olsen, B. B. Kragelund

The paper investigates the role of stereochemistry in disordered protein-protein interactions, finding that chirality is inconsequential in fully disordered complexes but essential when folding and binding are coupled.

bioRxiv · Feb 23, 2024 · PreprintBiophysics

A glutamine-based single α-helix scaffold to target globular proteins

A. Escobedo, J. G. Piccirillo, J. Aranda, T. Diercks, B. Topal, M. Biesaga, L. Staby, B. B. Kragelund, J. Garcia, O. Millet, M. Orozco, M. Coles, R. Crehuet, X. Salvatella

This paper introduces a method to design peptides that fold into single α-helices using glutamine side chain to main chain hydrogen bonds, enabling targeted interactions with globular proteins.

bioRxiv · May 6, 2022Biophysics