54580-47-1Relevant articles and documents
Bithiophenesulfonamide Building Block for π-Conjugated Donor-Acceptor Semiconductors
Melkonyan, Ferdinand S.,Zhao, Wei,Drees, Martin,Eastham, Nicholas D.,Leonardi, Matthew J.,Butler, Melanie R.,Chen, Zhihua,Yu, Xinge,Chang, Robert P. H.,Ratner, Mark A.,Facchetti, Antonio F.,Marks, Tobin J.
, p. 6944 - 6947 (2016)
We report here π-conjugated small molecules and polymers based on the new π-acceptor building block, bithiophenesulfonamide (BTSA). Molecular orbital computations and optical, electrochemical, and crystal structure analyses illuminate the architecture and electronic structure of the BTSA unit versus other acceptor building blocks. Field-effect transistors and photovoltaic cells demonstrate that BTSA is a promising unit for the construction of π-conjugated semiconducting materials.
NOVEL MESITYLENE-CORED AMPHIPHILES AND USES THEREOF
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Paragraph 126; 127; 137; 138; 181; 182, (2018/02/28)
The present invention relates to a mesitylene-cored amphiphile, a method of preparing the same and a method of extraction, solubilization, stabilization, crystallization or analysis of a membrane protein using the same. When a mesitylene-cored compound according to the present invention is used, membrane proteins can be stored in a stable conformation for a long time in an aqueous solution in comparison with conventional compounds, by which the membrane proteins are usable in both functional and structural analyses thereof. The functional and structural analyses of membrane proteins are one of the fields that are most spotlighted in current biology and chemistry. The present invention can be used to research on a protein structure closely related to new drug development.
Mesitylene-Cored Glucoside Amphiphiles (MGAs) for Membrane Protein Studies: Importance of Alkyl Chain Density in Detergent Efficacy
Cho, Kyung Ho,Ribeiro, Orquidea,Du, Yang,Tikhonova, Elena,Mortensen, Jonas S.,Markham, Kelsey,Hariharan, Parameswaran,Loland, Claus J.,Guan, Lan,Kobilka, Brian K.,Byrne, Bernadette,Chae, Pil Seok
supporting information, p. 18833 - 18839 (2016/12/26)
Detergents serve as useful tools for membrane protein structural and functional studies. Their amphipathic nature allows detergents to associate with the hydrophobic regions of membrane proteins whilst maintaining the proteins in aqueous solution. However