A6501
N-乙酰基-L-色氨酸酰胺
≥98%
别名:
NATA
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关于此项目
经验公式（希尔记法）:
C13H15N3O2
化学文摘社编号:
分子量:
245.28
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.26
EC Number:
219-189-8
MDL number:
产品名称
N-乙酰基-L-色氨酸酰胺,
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-乙酰基-L-色氨酰胺（NATA）是L-色氨酸的N端和C端封闭的类似物。L-色氨酸、NATA和NATA-tyr分子具有固有荧光，这使其适用于涉及荧光和荧光增强的研究中。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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
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
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
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