Arshdeep Sidhu

Dr. Arshdeep Sidhu is a protein biochemist with a specialization in single molecule/conformation imaging using atomic force microscopy. Her research interest includes studying conformation-function of intrinsically disordered proteins and to develop protein-based materials for diverse applications.

She did her PhD from University of Twente, The Netherlands, where she studied polymorphism and functionalization of a Parkinson’s disease associated protein – α-Synuclein. During her postdoctoral fellowship at Erasmus Medical Centre, Rotterdam, she studied the conformation-function relation of BRCA2 protein – a protein associated with breast cancer.

In addition to her research interests, Dr. Sidhu likes to travel, learn new skills and is an environmentalist, who actively seeks and implements solutions for everyday sustainable living.

We aim to understand how intrinsically disordered proteins self-assemble into functional (DNA repair foci/cancer) as well as pathogenic structures (protein aggregates/neurodegeneration). We are passionate about developing physiologically relevant in-vitro model systems that will enable single molecule studies of DNA repair foci and liquid to solid transition of amyloidogenic proteins. Such model systems are valuable tools to annotate clinical variants and guide clinical decision for age-associated diseases like cancer and neurodegeneration in the long-term.

Current Projects

Developing PML body-based model system for homologous recombination repair of dsDNA breaks (Startup Research Grant - 2024-2026)

Aditya Iyer, Arshdeep Sidhu and Vinod Subramaniam. How important is the N-terminal acetylation of alpha-synuclein for its function and aggregation into amyloids? Frontiers in Neuroscience. 2022; 16, 16:1003997.

M. Paul*, Arshdeep Sidhu*, H. Sánchez, S.E. van Rossum-Fikkert, Claire Wyman. BRCA2 diffusion and conformation linked to DNA repair function: Importance of the C-terminal domains. eLife 2021;10:e67926 * Equal contribution.

Arshdeep Sidhu, M. Grosbart, H. Sánchez, B. Verhagen, N.L.L. van der Zon, D. Ristić, S.E. van Rossum-Fikkert and Claire Wyman. Conformational flexibility and oligomerization of BRCA2 regions induced by RAD51 interaction. Nucleic Acids Research. 2020; 48 (17), 9649–9659.

Arshdeep Sidhu*, J. Vaneyck, C. Blum, Ine Segers-Nolten* and V. Subramaniam. Polymorph-specific distribution of binding sites determines thioflavin-T fluorescence intensity in α-synuclein fibrils. Amyloid. 2018; 25(3), 189-196. *Corresponding authors.

Arshdeep Sidhu, I. Segers-Nolten, V. Raussens, M.M.A.E. Claessens and Vinod Subramaniam. Distinct mechanisms determine α-synuclein fibril morphology during growth and maturation. ACS Chemical Neuroscience. 2017; 8(3): 538-547.

Arshdeep Sidhu, I. Segers-Nolten and Vinod Subramaniam. Conformational compatibility is essential for heterologous aggregation of α-synuclein. ACS Chemical Neuroscience. 2016; 7(6): 719-727.

Christian C. Raiss, T.S. Braun, I.B.M. Konings, H. Grabmayr, G.C. Hassink, A. Sidhu, J. le Feber, A.R. Bausch, C. Jansen, V. Subramaniam and Mireille M.A.E. Claessens. Functionally different Lewy Body-like inclusions yield insight into Parkinson's disease pathology. Scientific Reports. 2016; 6: 23116.

Arshdeep Sidhu, I. Segers-Nolten and Vinod Subramaniam. Solution conditions define morphological homogeneity of α-synuclein fibrils. BBA Proteins and Proteomics. 2014; 1844(12): 2127–34.

Arshdeep Sidhu, A. Surolia, A.D. Robertson and Monica Sundd. A hydrogen bond regulates slow motions in ubiquitin by modulating a β-turn flip. Journal of Molecular Biology. 2011; 411(5): 1037-48.