Anita Dutt

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Single crystal X-ray diffraction studies show that the extended structure of dipeptide Boc-beta-Ala-m-ABA-OMe (m-ABA: meta-aminobenzoic acid) self-assembles in the solid state by intermolecular hydrogen bonding to create an infinite parallel beta-sheet structure. In dipeptide Boc-gamma-Abu-m-ABA-OMe (gamma-Abu: gamma-aminobutyric acid), two such parallel(More)
Mitochondrial diseases are extremely heterogeneous multisystem disorders predominantly affecting tissues or organs with high oxygen consumption like skeletal muscles, brain, endocrine glands, myocardium, eyes, ears, intestines, liver, kidneys, and bone marrow. Although various clinical syndromes have been described, they frequently overlap and there is no(More)
Three structurally different types of small peptides, namely, i) Boc-Ile-Aib-Ile-OMe (Aib=alpha-aminoisobutyric acid), ii) Boc-Xx-m-aminobenzoic acid (Xx=beta-Ala and gamma-aminobutyric acid), and iii) Boc-Xx-m-nitroaniline, were found to exhibit beta-sheet-mediated fibrillogenesis in the solid state, revealed by FT-IR, single-crystal X-ray diffraction, and(More)
A single crystal X-ray diffraction study of the tripeptide Boc-Phe-Aib-Leu-OMe (Aib = alpha-aminoisobutyric acid) reveals that it forms structurally one of the best type II beta-turns so far reported in tripeptides, stabilized by 10 atom intramolecular hydrogen bonding. In contrast, the isomeric tripeptide Boc-Phe-Leu-Aib-OMe adopts a beta-strand like(More)
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