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Merck
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Documentos

A6501

Sigma-Aldrich

N-Acetyl-L-tryptophanamide

≥98%

Sinónimos:

NATA

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About This Item

Fórmula empírica (notación de Hill):
C13H15N3O2
Número de CAS:
2382-79-8
Peso molecular:
245.28
EC Number:
219-189-8
MDL number:
MFCD00005646
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
24891094
NACRES:
NA.26

product name

N-Acetyl-L-tryptophanamide,

assay

≥98%

form

powder

color

white to off-white

mp

194-196 °C (lit.)

application(s)

detection

storage temp.

−20°C

SMILES string

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

InChI key

HNGIZKAMDMBRKJ-LBPRGKRZSA-N

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Biochem/physiol Actions

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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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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
Billie J Harvey et al.
The journal of physical chemistry. B, 111(10), 2610-2620 (2007-02-16)
Bovine beta-lactoglobulin A (BLGA) is a well characterized globular protein whose tertiary structure has been investigated in detail. BLGA undergoes a pH-dependent conformational change which X-ray data described as involving mostly the loop connecting strands E and F and the
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