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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%

Quality Level

200

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)

Certificados de análisis (COA)

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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
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
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
A Buzády et al.
Biophysical chemistry, 88(1-3), 153-163 (2001-01-11)
The dielectric relaxation (DR) of human serum albumin (HSA) was studied by the method of phase-fluorometry. The protein environment of the single tryptophan in HSA shows a relatively low-speed DR of sub-ns characteristic time. This relaxation can be measured as
Jianhua Xu et al.
The journal of physical chemistry. B, 113(35), 12084-12089 (2009-08-28)
Time-resolved fluorescence decay profiles of N-acetyl-l-tryptophanamide (NATA) and tryptophan (Trp) dipeptides of the form Trp-X and X-Trp, where X is another aminoacyl residue, have been investigated using an ultraviolet upconversion spectrophoto fluorometer with time resolution better than 350 fs, together
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