Journal of computational chemistry, 25(7), 921-934 (2004-03-18)
Accurate and fast evaluation of electrostatic interactions in molecular systems is still one of the most challenging tasks in the rapidly advancing field of macromolecular chemistry, including molecular recognition, protein modeling and drug design. One of the most convenient and
A general approach to dissecting the complex photophysics of tryptophan is presented and used to elucidate the effects of amino acid functional groups on tryptophan fluorescence. We have definitively identified the amino acid side chains that quench tryptophan fluorescence and
Journal of the American Chemical Society, 130(12), 4089-4096 (2008-03-07)
Eight B-containing compounds, i.e., 1a-h, were prepared as mimics of the green fluorescent protein (GFP) fluorophore. The underlying concept was that synthetic GFP chromophore analogues are not fluorescent primarily because of free rotation about an aryl-alkene bond (Figure 1b). This
The journal of physical chemistry. A, 116(8), 1956-1965 (2012-01-26)
Within the structure determination task for peptides, which is of large interest due to the relation between structure and functionality, infrared spectra can provide detailed information on the conformational behavior. The conformational landscape ofN-acetylgycine has been studied by a combined
Journal of colloid and interface science, 314(2), 689-698 (2007-06-26)
The well-characterized, monodisperse nature of reverse micelles formed by sodium bis-(2-ethylhexyl)sulfosuccinate/water/isooctane and their usefulness in assimilating compounds of varied interests have been exploited to investigate the effect of acetyl modified amino acids (MAA) viz., N-acetyl-L-glycine (NAG), N-acetyl-L-aspartic acid (NAA) and
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