How Pulling Forces Tune Redox Potentials of Disulfide Bonds
نویسندگان
چکیده
منابع مشابه
Tunable nanomechanics of protein disulfide bonds in redox microenvironments.
Disulfide bonds are important chemical cross-links that control the elasticity of fibrous protein materials such as hair, feather, wool and gluten in breadmaking dough. Here we present a novel computational approach using the first-principles-based ReaxFF reactive force field and demonstrate that this approach can be used to show that the fracture strength of disulfide bonds is decreased under ...
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A scanning tunnelling microscope is used to pull a polythiophene wire from a Au(111) surface while measuring the current traversing the junction. Abrupt current increases measured during the lifting procedure are associated with the detachment of molecular subunits, in apparent contradiction with the expected exponential decrease of the conductance with wire length. Ab initio simulations reprod...
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Glutaredoxins belong to the thioredoxin superfamily of structurally similar thiol-disulfide oxidoreductases catalyzing thiol-disulfide exchange reactions via reversible oxidation of two active-site cysteine residues separated by two amino acids (CX1X2C). Standard state redox potential (E degrees ') values for glutaredoxins are presently unknown, and use of glutathione/glutathione disulfide (GSH...
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The inter- and intrasubunit disulfide bridges for the 11 S form of acetylcholinesterase isolated from Torpedo californica have been identified. Localized within the basal lamina of the synapse, the dimensionally asymmetric forms of acetylcholinesterase contain either two (13 S) or three (17 S) sets of catalytic subunits linked to collagenous and noncollagenous structural subunits. Limited prote...
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Due to some important applications of guanine electrode in scientific and technology research such as electro-chemical DNA based biosensors, and a problem of high redox potential of guanine (0.81 V), our research study concentrates on reducing guanine redox potential by substituting Cu, Ag, Au, CH3, C2H5 and Cl on sites of 1, 2 and 9 of guanine. A 5.0% reduction...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2011
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2010.12.353