N-Acetyl-L-tryptophanamide (NATA) is an N-terminal and C-terminal blocked analogue of L-tryptophan. L-tryptophan, NATA and NATA-tyr molecules have intrinsic fluorescence which makes them useful in studies involving fluorescence and flurosence enhancement.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Sugars are known to stabilize proteins. This study addresses questions of the nature of sugar and proteins incorporated in solid sugar films. Infrared (IR) and Raman spectroscopy was used to examine trehalose and sucrose films and glycerol/water solvent. Proteins and
Extremophiles : life under extreme conditions, 22(5), 781-793 (2018-07-18)
The biotechnological and industrial uses of thermostable and organic solvent-tolerant enzymes are extensive and the investigation of such enzymes from microbiota present in oil reservoirs is a promising approach. Searching sequence databases for esterases from such microbiota, we have identified
The Journal of chemical physics, 120(1), 133-147 (2004-07-23)
The conformational isomerization dynamics of N-acetyl tryptophan methyl amide (NATMA) and N-acetyl tryptophan amide (NATA) have been studied using the methods of IR-UV hole-filling spectroscopy (HFS) and IR-induced population transfer spectroscopy (IR-PTS), which were developed for this purpose. Single conformations
The Journal of biological chemistry, 279(47), 48680-48691 (2004-09-07)
2-O-alpha-Mannosylglycerate, a negatively charged osmolyte widely distributed among (hyper)thermophilic microorganisms, is known to provide notable protection to proteins against thermal denaturation. To study the mechanism responsible for protein stabilization, pico-second time-resolved fluorescence spectroscopy was used to characterize the thermal unfolding
Evaporation of water from a 1/1 mixture of trehalose and sucrose gives rise to optically clear glasses that are transparent in the UV and visible ranges and do not crystallize when they are prepared at ambient temperatures. Two proteins, liver
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