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Gopa Mitra

Researcher at St. John's University

Publications -  25
Citations -  385

Gopa Mitra is an academic researcher from St. John's University. The author has contributed to research in topics: Hemoglobin & Hydrogen–deuterium exchange. The author has an hindex of 10, co-authored 24 publications receiving 325 citations. Previous affiliations of Gopa Mitra include St. John's Medical College & Indian Institute of Science.

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Sulfonamide drugs binding to the colchicine site of tubulin: thermodynamic analysis of the drug-tubulin interactions by isothermal titration calorimetry.

TL;DR: It is demonstrated that these sulfonamide drugs bind to the colchicine site of tubulin in a reversible manner and indicate that a mere alteration in the position of a single substituent chlorine on the indole scaffold has a great influence on the drug-tubulin binding thermodynamics.
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Conformational heterogeneity of tau: Implication on intrinsic disorder, acid stability and fibrillation in Alzheimer's disease.

TL;DR: The observations at low pH indicate that a reorganization of the intricate network of momentary long-range contacts in tau might have implication in its aggregation pathology, and nano-electrospray mass spectrometry coupled with ion mobility provides a direct insight into the ensemble of highly heterogeneous conformational families of tau at physiological pH.
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Beneficiary effect of nanosizing ferric pyrophosphate as food fortificant in iron deficiency anemia: evaluation of bioavailability, toxicity and plasma biomarker

TL;DR: The nanoparticle ferric pyrophosphate could be a promising food fortificant in combating iron deficiency anemia, while Fetuin-B, a negative acute phase protein, might be a potential candidate for detecting biological responses to the nanoparticle exposure in vivo.
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Glutathionylation induced structural changes in oxy human hemoglobin analyzed by backbone amide hydrogen/deuterium exchange and MALDI-mass spectrometry.

TL;DR: This study investigated the effects of glutathionylation on quaternary structure of hemoglobin using hydrogen/deuterium exchange (H/DX) based mass spectrometry to understand structural perturbation on post-translational modification of proteins in solution phase.
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Application of native mass spectrometry in studying intrinsically disordered proteins: A special focus on neurodegenerative diseases

TL;DR: The advantages of native mass spectrometry (MS) in analysing the atypical conformational dynamics of IDPs and recent advances made in the field are discussed.