product name
N-乙酰基-L-色氨酸酰胺,
检测方案
≥98%
质量水平
形式
powder
颜色
white to off-white
mp
194-196 °C (lit.)
应用
detection
储存温度
−20°C
SMILES字符串
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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生化/生理作用
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。
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
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
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
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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