Results 41 to 50 of about 260,568 (212)
Disulfide-Catalyzed Iodination of Electron-Rich Aromatic Compounds
, 2019 Herein, a disulfide-catalyzed electrophilic iodination of aromatic compounds using 1,3-diiodo-5,5-dimethylhydantoin (DIH) has been developed. The disulfide activates DIH as a Lewis base to promote the iodination reaction in acetonitrile under mild ...
Takamichi Watanabe +7 more
core +1 more source
Disulfide-Strapped Porphyrins for Monolayer Formation on Gold
, 2016 Porphyrins with a disulfide-containing strap have been prepared as an alternative to dithiols for self-assembled monolayer formation on gold surfaces. The strapped porphyrins have the advantage of greater air stability than their dithiol analogues.
James E. Redman (362293) +1 more
core +1 more source
Disulfide-Driven Cyclic Peptide Synthesis of Human Endothelin‑2 with a Solid-Supported Npys-Cl
, 2019 We report here the synthesis of human endothelin-2, a peptide of 21 amino acid residues with two disulfide bonds, based on the novel idea of a disulfide-driven cyclic peptide synthesis (DdCPS).
Atsuhiko Taniguchi (2653804) +5 more
core +1 more source
Folding of peptides and proteins: role of disulfide bonds, recent developments
Biomolecular Concepts, 2013 Disulfide-containing proteins are ideal models for studies of protein folding as the folding intermediates can be observed, trapped, and separated by HPLC during the folding reaction.
Hidaka Yuji, Shimamoto Shigeru
doaj +1 more source
Origin of Structural Transformation in Mono- and Bi-Layered Molybdenum Disulfide
, 2016 Mono- and multi-layered molybdenum disulfide (MoS2) is considered to be one of the next generation anode materials for rechargeable ion batteries.
Sun, Xiaoli +3 more
core +1 more source
FEBS Letters, 2013 Improving the stability of proteins is an important goal in many biomedical and industrial applications. A logical approach is to emulate stabilizing molecular interactions found in nature. Disulfide bonds are covalent interactions that provide substantial stability to many proteins and conform to well‐defined geometric conformations, thus making them ...
Dombkowski, Alan A. +2 more
openaire +2 more sources
Protein Engineering Design and Selection, 2003 The formation of a disulfide bond between adjacent cysteine residues is accompanied by the formation of a tight turn of the protein backbone. In nearly 90% of the structures analyzed a type VIII turn was found. The peptide bond between the two cysteines is in a distorted trans conformation, the omega torsion angle ranges from 159 to -133 degrees, with ...
Carugo, O. +6 more
openaire +6 more sources
Microbiology Spectrum, 2023 The bacterium Bacillus subtilis is of high importance both as a model organism for Gram-positive bacteria and as an industrial workhorse in the production of biomolecules.
Jonathan Walgraeve +6 more
doaj +1 more source
Metal bridges to probe membrane ion channel structure and function
Biomolecular Concepts, 2015 Ion channels are integral membrane proteins that undergo important conformational changes as they open and close to control transmembrane flux of different ions.
Linsdell Paul
doaj +1 more source
Physicochemical properties that control protein aggregation also determine whether a protein is retained or released from necrotic cells [PDF]
Open Biology, 2016 Amyloidogenic protein aggregation impairs cell function and is a hallmark of many chronic degenerative disorders. Protein aggregation is also a major event during acute injury; however, unlike amyloidogenesis, the process of injury-induced protein ...
Andre L. Samson +7 more
doaj +1 more source