Author

S. Nerli

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 Biophysics· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Assay:structural biology· 2 Approach:deep learning· 1 Research Focus:protein design· 1 Research Focus:protein structure prediction· 1 Approach:statistical model· 1

Frequent Co-Authors

N. G. Sgourakis· 3 shared A. C. McShan· 1 shared A. K. Kancherla· 1 shared C. R. Glassman· 1 shared D. A. Fletcher· 1 shared D. Baker· 1 shared D. Moschidi· 1 shared D. P. Dowling· 1 shared

Activity by Year

2019-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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3 shared papersBiochemistry

N. G. Sgourakis

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Author profile →

4 papers

Recent·Most cited

Global Dynamics as Communication Sensors in Peptide Synthetase Cyclization Domains.

S. H. Mishra, A. K. Kancherla, K. A. Marincin, G. Bouvignies, S. Nerli, N. Sgourakis, D. P. Dowling, D. P. Frueh

The paper uses NMR to show that global dynamics in NRPS cyclization domains act as sensors for substrate interactions, enabling allosteric responses across the enzyme.

bioRxiv · Oct 6, 2021 · PreprintBiophysics

Structure-based modeling of SARS-CoV-2 peptide/HLA-A02 antigens

S. Nerli, N. G. Sgourakis

The paper uses RosettaMHC to model SARS-CoV-2 peptide/HLA-A02 antigens and makes the models publicly available.

bioRxiv · Mar 23, 2020Immunology

Interleukin-2 druggability is modulated by global conformational transitions controlled by a helical capping switch

V. S. De Paula, K. M. Jude, S. Nerli, C. R. Glassman, K. C. Garcia, N. G. Sgourakis

This study identifies a helical capping switch in IL-2 that modulates its conformational transitions and drug interactions, providing a framework for designing precision therapeutics.

bioRxiv · Oct 28, 2019Biochemistry

Computational design of a protein family that adopts two well-defined and structurally divergent de novo folds

K. Y. Wei, D. Moschidi, M. J. Bick, S. Nerli, A. C. McShan, L. P. Carter, P.-S. Huang, D. A. Fletcher, N. G. Sgourakis, S. E. Boyken, D. Baker

This paper designs a protein family with two structurally divergent folds, showing that sequences can adopt distinct conformations under different conditions.

bioRxiv · Sep 4, 2019 · PreprintBiochemistry