Author

Diamond Jain

Indian Institute of Technology KharagpurORCID 0009-0005-5022-7777Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Microbiology· 2 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:proteomics· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:development & morphogenesis· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

Anindya Sundar GhoshiD· 3 shared Tejavath AjithiD· 2 shared Bayomi BijuiD· 1 shared Chiranjit ChowdhuryiD· 1 shared Debasmita ChatterjeeiD· 1 shared Gaurav KumariD· 1 shared Jyoti Kumar VermaiD· 1 shared Sarmistha BiswaliD· 1 shared

Activity by Year

2024-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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3 shared papersMicrobiology

Anindya Sundar GhoshORCID

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3 papers

Recent·Most cited

Molecular BiologybioRxivPreprintMay 23, 2026

Deciphering the role of the non-active site ancillary residues in maintaining the activity and substrate specificity of OXA-232 beta-lactamase

Tejavath Ajith, Bayomi Biju, Diamond Jain…·Anindya Sundar Ghosh

This study investigates the role of non-active site residues in OXA-232 beta-lactamase, showing their impact on activity, substrate specificity, and structural stability through site-directed mutagenesis and biophysical analysis.

DOI 10.64898/2026.05.22.727341

experimental assay

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MicrobiologyFEMS Microbiology LettersPeer-reviewedJan 1, 2025

Conserved ancillary residues situated proximally to the VIM-2 active site affect its metallo β-lactamase activity

Diamond Jain, Tejavath Ajith, Jyoti Kumar Verma…·Anindya Sundar Ghosh

The paper investigates the impact of specific amino acid substitutions near the VIM-2 active site on its metallo β-lactamase activity and stability, finding that N210A and D182A reduce catalytic efficiency and thermal stability.

1 citation

proteomicsexperimental assay

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MicrobiologyFEMS Microbiology LettersPeer-reviewedJan 1, 2024

Acinetobacter baumannii DacC influences cell shape, biofilm formation, and physiological fitness by manifesting DD-carboxypeptidase and β-lactamase dual-enzyme activities

Shilpa Pal, Diamond Jain, Sarmistha Biswal…·Anindya Sundar Ghosh

This study identifies DacC in Acinetobacter baumannii as a dual-enzyme with DD-carboxypeptidase and β-lactamase activities that affect cell shape, biofilm formation, and antibiotic susceptibility.

2 citations

bacteria (other)proteomics

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