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Documentos

A6501

Sigma-Aldrich

N-Acetyl-L-tryptophanamide

≥98%

Sinônimo(s):

NATA

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About This Item

Fórmula empírica (Notação de Hill):
C13H15N3O2
Número CAS:
2382-79-8
Peso molecular:
245.28
Número CE:
219-189-8
Número MDL:
MFCD00005646
Código UNSPSC:
12352209
eCl@ss:
32160406
ID de substância PubChem:
24891094
NACRES:
NA.26

product name

N-Acetyl-L-tryptophanamide,

Ensaio

≥98%

forma

powder

cor

white to off-white

pf

194-196 °C (lit.)

aplicação(ões)

detection

temperatura de armazenamento

−20°C

cadeia de caracteres SMILES

CC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(N)=O

InChI

1S/C13H15N3O2/c1-8(17)16-12(13(14)18)6-9-7-15-11-5-3-2-4-10(9)11/h2-5,7,12,15H,6H2,1H3,(H2,14,18)(H,16,17)/t12-/m0/s1

chave InChI

HNGIZKAMDMBRKJ-LBPRGKRZSA-N

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Ações bioquímicas/fisiológicas

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.

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)

Certificados de análise (COA)

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Tiago Q Faria et al.
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
Qiang Li et al.
Analytical biochemistry, 367(1), 104-110 (2007-06-08)
We present a label-free detection of protein interaction between beta-galactosidase from Escherichia coli (Ecbeta-Gal) and monoclonal anti-Ecbeta-Gal using deep UV laser-based fluorescence lifetime microscopy. The native fluorescence from intrinsic tryptophan emission was observed after one-photon excitation at 266 nm. Applying
Patrizia Cioni et al.
Biophysical journal, 82(6), 3246-3253 (2002-05-23)
The effects of heavy water (D(2)O) on internal dynamics of proteins were assessed by both the intrinsic phosphorescence lifetime of deeply buried Trp residues, which reports on the local structure about the triplet probe, and the bimolecular acrylamide phosphorescence quenching
Alexander V Fonin et al.
PloS one, 9(7), e103878-e103878 (2014-07-30)
Fluorescence is a proven tool in all fields of knowledge, including biology and medicine. A significant obstacle in its use is the nonlinearity of the dependence of the fluorescence intensity on fluorophore concentration that is caused by the so-called primary
A Mozo-Villarías
Journal of biochemical and biophysical methods, 50(2-3), 163-178 (2001-12-14)
The second derivatives of N-acetyl-L-tryptophan amide (AcTrpNH(2)) fluorescence spectra were characterised in order to describe changes in the tryptophan environments of proteins. This tryptophan model compound was studied in several media with different degrees of hydrophobicity. The effect of tyrosines
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