Nicholus Bhattacharjee

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Hydration layer water molecules play important structural and functional roles in proteins. Despite being a critical component in biomolecular systems, characterizing the properties of hydration water poses a challenge for both experiments and simulations. In this context we investigate the local structure of hydration water molecules as a function of the(More)
Background: Analysis of known protein structures reveals that identical sequence fragments in proteins can adopt different secondary structure conformations. The extent of this conformational diversity is influenced by various factors like the intrinsic sequence propensity, sequence context and other environmental factors such as pH, site directed mutations(More)
Water on a protein surface plays a key role in determining the structure and dynamics of proteins. Compared to the properties of bulk water, many aspects of the structure and dynamics of the water surrounding the proteins are less understood. It is interesting therefore to explore how the properties of the water within the solvation shell around the peptide(More)
This work is a first attempt to characterise the conformational preference of structurally ambivalent helices in terms of their backbone conformational entropy. Ambivalent sequences conform to two different secondary structures (helix-sheet or helix-random coil or sheet-random coil, etc.) in two different proteins. For variable ambivalent helices, the(More)
BACKGROUND Despite the importance of β-strands as main building blocks in proteins, the propensity of amino acid in β-strands is not well-understood as it has been more difficult to determine experimentally compared to α-helices. Recent studies have shown that most of the amino acids have significantly high or low propensity towards both ends of β-strands.(More)
Secondary structural elements like alpha-helix and beta-sheet constitute the major components of proteins. Here we present a systematic position wise analysis of the structural and sequence characteristics of alpha-helices and beta-sheets. Helix and sheet are found to follow a complementary distribution pattern along the protein chain length. We have(More)
BACKGROUND Analysis of known protein structures reveals that identical sequence fragments in proteins can adopt different secondary structure conformations. The extent of this conformational diversity is influenced by various factors like the intrinsic sequence propensity, sequence context and other environmental factors such as pH, site directed mutations(More)
The synthesis of all-cis amide (NtBu)-glycine oligomers up to 15 residues long by a blockwise coupling approach is reported. The structure and dynamical behavior of these peptoids have been studied by X-ray crystallography, NMR and molecular modeling. Analyses reveal that the folding of these oligomers is driven by weak CH···O=C hydrogen bonding along the(More)
This paper reports on a microfluidic device with high spatiotemporal control used as an in vitro model of neuromuscular junction (NMJ) developmental biology. The device is assembled using three poly(dimethylsiloxane) (PDMS) layers and consists of micro-trenches for long-term culture of myotubes and an array of 32 identical focal stimulation jets to(More)
The l,d-transpeptidases, Ldts, catalyze peptidoglycan cross-linking in β-lactam-resistant mutant strains of several bacteria, including Enterococcus faecium and Mycobacterium tuberculosis. Although unrelated to the essential d,d-transpeptidases, which are inactivated by the β-lactam antibiotics, they are nevertheless inhibited by the carbapenem antibiotics,(More)