Redox Potentials of Protein Disulfide Bonds from Free-Energy Calculations
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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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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Disulfide bonds play an important role in protein folding and stability. However, the cross-linking of sites within proteins by cysteine disulfides has significant distance and dihedral angle constraints. Here we report the genetic encoding of noncanonical amino acids containing long side-chain thiols that are readily incorporated into both bacterial and mammalian proteins in good yields and wi...
متن کاملDisulfide bonds as switches for protein function.
The prevailing view is that disulfide bonds have been added during evolution to enhance the stability of proteins that function in a fluctuating cellular environment. However, recent evidence indicates that disulfide bonds can be more than inert structural motifs. The function of some secreted soluble proteins and cell-surface receptors is controlled by cleavage of one or more of their disulfid...
متن کاملThe Effect of Tensile Stress on the Conformational Free Energy Landscape of Disulfide Bonds
Disulfide bridges are no longer considered to merely stabilize protein structure, but are increasingly recognized to play a functional role in many regulatory biomolecular processes. Recent studies have uncovered that the redox activity of native disulfides depends on their C-C-S-S dihedrals, χ2 and χ'2. Moreover, the interplay of chemical reactivity and mechanical stress of disulfide switches ...
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ژورنال
عنوان ژورنال: The Journal of Physical Chemistry B
سال: 2015
ISSN: 1520-6106,1520-5207
DOI: 10.1021/acs.jpcb.5b01051