Results 341 to 350 of about 1,312,330 (378)
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Biochemistry, 2006
Disulfide bonds have been generally considered to be either structural or catalytic. Structural bonds stabilize a protein, while catalytic bonds mediate thiol-disulfide interchange reactions in substrate proteins. There is emerging evidence for a third type of disulfide bond that can control protein function by triggering a conformational change when ...
Bryan Schmidt +2 more
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Disulfide bonds have been generally considered to be either structural or catalytic. Structural bonds stabilize a protein, while catalytic bonds mediate thiol-disulfide interchange reactions in substrate proteins. There is emerging evidence for a third type of disulfide bond that can control protein function by triggering a conformational change when ...
Bryan Schmidt +2 more
openaire +3 more sources
Disulfide Bond-Driven Oxidation- and Reduction-Responsive Prodrug Nanoassemblies for Cancer Therapy.
Nano letters (Print), 2018Disulfide bonds have been widely used to develop reduction-responsive drug-delivery systems (DDS) for cancer therapy. We propose that disulfide bonds might be also used as an oxidation-responsive linkage just like thioether bonds, which can be oxidized ...
Bingjun Sun +11 more
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Angewandte Chemie, 2019
One of the applied synthetic strategies for correct disulfide bond formation relies on the use of orthogonal Cys protecting groups. This approach requires purification before and after the deprotection steps, which prolongs the entire synthetic process ...
Shay Laps +3 more
semanticscholar +1 more source
One of the applied synthetic strategies for correct disulfide bond formation relies on the use of orthogonal Cys protecting groups. This approach requires purification before and after the deprotection steps, which prolongs the entire synthetic process ...
Shay Laps +3 more
semanticscholar +1 more source
MAKING AND BREAKING DISULFIDE BONDS
Annual Review of Microbiology, 1997▪ Abstract It is now well established that protein folding requires the assistance of folding helpers in vivo. The formation or isomerization of disulfide bonds in proteins is a slow process requiring catalysis. In nascent polypeptide chains the cysteine residues are in the thiol form.
Dominique Missiakas, Satish Raina
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Disulfide Bond Formation in the Cytoplasm
Antioxidants & Redox Signaling, 2013Disulfide bond formation is critical for biogenesis of many proteins. While most studies in this field are aimed at elucidating the mechanisms in the endoplasmic reticulum, intermembrane space of mitochondria, and prokaryotic periplasm, structural disulfide bond formation also occurs in other compartments including the cytoplasm.
Lloyd W. Ruddock, Mirva J. Saaranen
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Disulfide Bond Exchange in Rhodopsin
Biochemistry, 1998Rhodopsin contains two cysteines (Cys110 and Cys187) that are highly conserved among members of the G protein coupled receptor family and that form a disulfide bond connecting helixes 3 and 4 on the extracellular side of the protein. However, recent work on a rhodopsin mutant split in the cytoplasmic loop connecting helixes 3 and 4 has shown that the ...
Daniel D. Oprian +2 more
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The Characteristics of Disulfide‐Centered Hydrogen Bonds
Angewandte Chemie, 2021AbstractThe disulfide‐centered hydrogen bonds in the three different model systems of diethyl disulfide⋅⋅⋅H2O/H2CO/HCONH2 clusters were characterized by high‐resolution Fourier transform microwave spectroscopy and quantum chemical computations. The global minimum energy structures for each cluster are experimentally observed and are characterized by ...
Tao Lu +7 more
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ACS Chemical Biology, 2015
Lasso peptides are bacterial ribosomally synthesized and post-translationally modified peptides. They have sparked increasing interest in peptide-based drug development because of their compact, interlocked structure, which offers superior stability and ...
Yanyan Li +10 more
semanticscholar +1 more source
Lasso peptides are bacterial ribosomally synthesized and post-translationally modified peptides. They have sparked increasing interest in peptide-based drug development because of their compact, interlocked structure, which offers superior stability and ...
Yanyan Li +10 more
semanticscholar +1 more source
The disulfide bond in carboxypeptidase A: A
Biochemical and Biophysical Research Communications, 1969Abstract Carboxypeptidase A was assayed for active sulfhydryl groups by titration with HgCl 2 . A chloride ion probe NMR technique was utilized to observe the behavior of the mercuric ion. Although mercuric ion was found to bind to the enzyme, it could be removed by dialysis showing that the binding cannot be through a sulfur atom.
Thomas R. Stengle +2 more
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