Publications by authors named "Prasun Pal"
Bacteria containing ice-nucleating proteins (INPs) evolved in nature to nucleate ice at the high sub-zero ambiance. The ability of the INPs to induce order in the hydration layer and their aggregation propensity appear to be key factors of their ice nucleation abilities. However, the mechanism of the process of ice nucleation by INPs is yet to be understood clearly.
View Article and Find Full Text PDFProteins function close to native and near-native conformations. These states are evolutionarily selected to ensure the effect of mutations is minimized. The structural organization of a protein is hierarchical and modular, which reduces the dimensionality of the configurational space of the native states.
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- The study investigates how antifreeze proteins (AFPs) inhibit ice growth by comparing a moderately active type III AFP and a hyperactive spruce budworm AFP, using molecular dynamics simulations.
- The results indicate that ice surface coverage is crucial for ice growth inhibition; higher coverage leads to stronger binding between AFPs and ice due to multiple hydrogen bonds.
- In low AFP concentration scenarios, AFPs can act like impurities instead, getting trapped in the growing ice crystal rather than preventing its growth.
Article Synopsis
- The article explores the supramolecular polymerization of two naphthalene-diimide (NDI) building blocks, NDI-L and NDI-C, in n-heptane and methylcyclohexane, highlighting how their different structures affect gel formation.
- Distinct internal orders and hydrogen bonding patterns were observed in both NDI types across solvents, with NDI-L forming a stronger gel in n-heptane, whereas NDI-C showed a preference for methylcyclohexane, which resulted in moderate gel strength.
- Molecular dynamics simulations and solvent-induced experiments demonstrated a crucial role of solvent shape-matching in influencing self-assembly and stability, revealing that solvent interactions are key to the properties of the resulting supramolecular polymers
Article Synopsis
- Antifreeze proteins (AFPs) prevent ice crystal growth by interacting specifically with ice surfaces, with hyperactive AFPs having a unique threonine-rich motif for binding.
- Research revealed that the hydration layer around the non-ice-binding surface (non-IBS) of hyperactive AFPs is liquid-like, contrasting with the ice-like hydration around the ice-binding surface (IBS), even in cold conditions.
- The study highlights differences in amino acid composition and arrangement between the IBS, non-IBS, and non-AFP surfaces, demonstrating how both surfaces work together to inhibit ice growth: the IBS for binding to ice and the non-IBS for preventing ice formation.