Gautam Basu

TL;DR: The location of the colchicine-binding site on tubulin by docking has been located on the α/β interface on the N-terminal side, which is also supported by much of the solution data, suggesting that influence of the tail region is transmitted by a pH-dependent conformational change.

TL;DR: In this article, the authors synthesized four dimeric peptides containing one fluorescent chromophore, β-(1'-naphthyl)-L-alanine or β-( 1'-nAPHthyl]-D-alanines, and one heavy atom perturber, p-bromo-L-phenylalanine, as two pairs of diastereoisomers-one cyclic pair and one linear pair.

TL;DR: The studies indicate that the interior of the caffeine dimer is well-solvated; however, the dynamics of solvation is retarted significantly compared to that in bulk water, clearly revealing the dimers maintain some ordered water molecules.

TL;DR: The unfolding transition of a short designed (α‐amino isobutyric acid/alanine‐based) helical peptide containing an interacting Tyr residue is studied to demonstrate that conformationally restricted aromatic side‐chains that interact with the helical backbone may also alter the unfolding profiles, monitored by far‐UV CD, rendering them unfit for a simple analysis for extracting the appropriate unfolding thermodynamic parameters.

TL;DR: A weak and nominally spin-forbidden singlet-triplet energy transfer and the remote heavy atom effect (RHAE) on the intersystem crossing within the fluorophore are established, which may have significance for the understanding of the role of helices in biological electron-transfer interactions.