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Neha Jain

Researcher at Indian Institute of Technology Delhi

Publications -  6
Citations -  95

Neha Jain is an academic researcher from Indian Institute of Technology Delhi. The author has contributed to research in topics: Protein folding & Equilibrium unfolding. The author has an hindex of 3, co-authored 6 publications receiving 82 citations. Previous affiliations of Neha Jain include Indian Institutes of Technology.

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Proceedings ArticleDOI

Gait recognition based on gait pal and pal entropy image

TL;DR: This paper proposes a novel temporal representation of Gait using Pal and Pal Entropy (GPPE) for each cycle of the silhouettes using Principal component analysis to create a feature matrix.
Journal ArticleDOI

Investigation of folding unfolding process of a new variant of dihydrofolate reductase protein from Zebrafish.

TL;DR: A comparative study of various species of DHFR shows that zDHFR has comparable thermodynamic stability with human counterpart and thus proved to be a good in vitro model system for structure- function relationship studies.
Journal ArticleDOI

Kinetics and thermodynamics of the thermal inactivation and chaperone assisted folding of zebrafish dihydrofolate reductase

TL;DR: Minichaperone can act as a very good in vitro as well as in vivo chaperone model for monitoring assisted protein folding phenomenon and indicates that it enhances the thermal stability of the enzyme.
Journal ArticleDOI

Comparison of physico-chemical aspects between E. coli and human dihydrofolate reductase: an equilibrium unfolding study

TL;DR: It was observed that 100 mM proline does not show any significant stabilization to either DHFRs and the human protein is relatively less stable than the E. coli counterpart.
Journal ArticleDOI

Minichaperone (GroEL191-345) mediated folding of MalZ proceeds by binding and release of native and functional intermediates.

TL;DR: Observations suggest that the minichaperone works by carrying out repeated cycles of binding aggregation-prone protein MalZ in a relatively compact conformation and in a partially folded but active state, and releasing them to attempt to fold in solution.