A6501
N-Acetyl-L-tryptophanamide
≥98%
Synonym(s):
NATA
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About This Item
Empirical Formula (Hill Notation):
C13H15N3O2
CAS Number:
Molecular Weight:
245.28
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.26
EC Number:
219-189-8
MDL number:
Product Name
N-Acetyl-L-tryptophanamide,
SMILES string
CC(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(N)=O
InChI key
HNGIZKAMDMBRKJ-LBPRGKRZSA-N
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
assay
≥98%
form
powder
color
white to off-white
mp
194-196 °C (lit.)
application(s)
detection
storage temp.
−20°C
Quality Level
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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
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
A Málnási-Csizmadia et al.
Biochemistry, 40(42), 12727-12737 (2001-10-17)
The fluorescence emission intensity from a conserved tryptophan residue (W501) located in the relay loop (F466 to L516) of the Dicytostelium discoideum myosin II motor domain is sensitive to ATP binding and hydrolysis. The initial binding process is accompanied by
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
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
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