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CAS

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66102-32-7

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66102-32-7 Usage

Chemical structure

Bicyclic, saturated heterocyclic compound

Family

Quinoxaline family

Physical state

Colorless to light yellow liquid

Odor

Faint

Uses

a. Fragrance ingredient in the cosmetic industry
b. Flavoring agent in the food industry

Therapeutic properties

a. Antioxidant effects
b. Anti-inflammatory effects

Precautions

Handle and use with caution due to potential health effects and hazards
Please note that this list is based on the provided material and may not cover all aspects of TMTQ. Further research and consultation with a professional chemist or toxicologist is recommended for a comprehensive understanding of the compound.

Check Digit Verification of cas no

The CAS Registry Mumber 66102-32-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 6,6,1,0 and 2 respectively; the second part has 2 digits, 3 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 66102-32:
(7*6)+(6*6)+(5*1)+(4*0)+(3*2)+(2*3)+(1*2)=97
97 % 10 = 7
So 66102-32-7 is a valid CAS Registry Number.

66102-32-7Downstream Products

66102-32-7Relevant articles and documents

Long-range electron transfer in rigid 310-helical oligopeptides containing redox cyclic α-amino acids

Lang, Kamil,Kuki, Atsuo

, p. 579 - 584 (1999)

Intrahelical photoinduced electron transfer processes (ET) in conformationally restricted oligopeptides have been studied by nanosecond time-resolved transient spectroscopy. The helical peptides were constructed from sterically hindered α-aminoisobutyric acid (Aib) and two cyclic α-amino acids (Aib class) bearing electron acceptor and donor side chains (DkNap, ThQx). This helical backbone design provides high conformation stability, as previously demonstrated, and yields reliable 310-helical architectures in solution. The forward ET between ThQx and 3DkNap is followed by a slow back ET thus giving rise to an accumulation of the charge-separated ion pairs for hundreds of nanoseconds. We demonstrate the modulation of electronic interactions by the number of intervening Aib residues separating acceptor-donor side chains and propose modifications of the peptide framework by inclusion of a non-Aib amino acid residue. These well-defined and sterically stable frameworks are suited for the precise evaluation of intrahelical electron transfer processes mediated by peptides.

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