Author

D. D. Prakashchand

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· 4

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 3 Assay:protein structure· 3 Approach:statistical model· 2 Approach:biophysical modeling· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

J. Mondal· 4 shared N. Ahalawat· 2 shared S. Sengupta· 2 shared H. Khandelia· 1 shared J. Koneru· 1 shared N. Dube· 1 shared P. Ghosh· 1 shared S. Bandyopadhyay· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

8 top collaborators · 15 mutual co-author links

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4 shared papersBiophysics

J. Mondal

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4 papers

Recent·Most cited

Spontaneous Transmembrane Pore Formation by Short-chain Synthetic Peptide

J. Koneru, D. D. Prakashchand, N. Dube, P. Ghosh, J. Mondal

This paper investigates how a short synthetic β-peptide forms transmembrane pores in lipid bilayers through molecular dynamics simulations, showing sequence-dependent pore formation and membrane disruption.

bioRxiv · Feb 12, 2021Biophysics

Conformational Reorganisation of Apolipoprotein E Triggered by Phospholipid Assembly

D. D. Prakashchand, J. Mondal

This paper uses molecular dynamics simulations to show that phospholipid binding induces conformational changes in apoE3, leading to an open structure that may facilitate receptor recognition.

bioRxiv · Aug 18, 2020 · PreprintBiophysics

Non-affine displacements encode collective conformational fluctuations in proteins

D. D. Prakashchand, N. Ahalawat, S. Bandyopadhyay, S. Sengupta, J. Mondal

The paper identifies non-affine displacements as key to resolving the free energy landscape of macromolecules using time-structured independent component analysis and Markov state models.

bioRxiv · Nov 20, 2019Biophysics

On identifying collective displacements in apo-proteins that reveal eventual binding pathways

D. D. Prakashchand, N. Ahalawat, H. Khandelia, J. Mondal, S. Sengupta

The paper identifies collective displacements in apo-proteins that correlate with binding pathways without requiring actual binding events.

bioRxiv · Jun 8, 2018Biophysics