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Merck
CN

A6501

Sigma-Aldrich

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
EC Number:
MDL number:
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.26
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Product Name

N-Acetyl-L-tryptophanamide,

Assay

≥98%

Quality Level

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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A Mozo-Villarías
Journal of biochemical and biophysical methods, 50(2-3), 163-178 (2001-12-14)
The second derivatives of N-acetyl-L-tryptophan amide (AcTrpNH(2)) fluorescence spectra were characterised in order to describe changes in the tryptophan environments of proteins. This tryptophan model compound was studied in several media with different degrees of hydrophobicity. The effect of tyrosines
Giovanni B Strambini et al.
Biophysical journal, 99(3), 944-952 (2010-08-05)
Quenching of Trp phosphorescence in proteins by diffusion of solutes of various molecular sizes unveils the frequency-amplitude of structural fluctuations. To cover the sizes gap between O(2) and acrylamide, we examined the potential of acrylonitrile to probe conformational flexibility of
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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