Author

Firdaus Samsudin

Agency for Science, Technology and ResearchORCID 0000-0003-2766-4459Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Bioinformatics· 2 Immunology· 1

Signature Assays, Organisms & Methods

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Research Focus:drug response / drug discovery· 2 Assay:protein structure· 2 Approach:statistical model· 2 Approach:Bayesian inference· 1 Organism:human· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Organism:virus· 1

Frequent Co-Authors

Peter John BondiD· 3 shared Alicia Ghia Min Ong· 1 shared Artur SchmidtcheniD· 1 shared Chinh Tran-To SuiD· 1 shared Di TangiD· 1 shared Enrico GuarneraiD· 1 shared Erik HartmaniD· 1 shared Igor N. BerezovskyiD· 1 shared

Activity by Year

2022-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBioinformatics

Peter John BondORCID

Mutual co-authors in cluster

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3 papers

Recent·Most cited

ImmunologybioRxivPreprintSep 18, 2026

Ara h 2 and FcϵRIα binding elicit state-dependent allostery in IgE

Mathialagan Mugundhan, Qinyu Jia, Palur Venkata Raghuvamsi…·Chinh Tran-To Su

This study investigates how Ara h 2 and FcϵRI binding affect IgE structural dynamics and allosteric communication, revealing conformational changes and shifts in communication pathways.

DOI 10.64898/2026.09.11.750994

protein structurestatistical model

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BioinformaticsbioRxivPreprintJan 20, 2025

Navigating the peptide sequence space in search for peptide binders with BoPep

Erik Hartman, Firdaus Samsudin, Malcolm Siljehag Alencar…·Johan A. Malmström

BoPep identifies peptide binders to specific proteins by efficiently navigating sequence space, reducing docking evaluations and discovering novel therapeutic peptides.

1 citation

humanproteomics

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BioinformaticsStructurePeer-reviewedJan 20, 2022

Allosteric perspective on the mutability and druggability of the SARS-CoV-2 Spike protein

Zhen Wah Tan, Wei-Ven Tee, Firdaus Samsudin…·Igor N. Berezovsky

The paper explores the role of allosteric mechanisms in the mutability and druggability of the SARS-CoV-2 Spike protein, identifying potential mutation sites and drug targets.

39 citationstop 4%

virusprotein structure

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