Nondissociative Electron Capture by Disulfide Bonds
نویسندگان
چکیده
منابع مشابه
Does Electron Capture Dissociation Cleave Protein Disulfide Bonds?
Peptide and protein characterization by mass spectrometry (MS) relies on their dissociation in the gas phase into specific fragments whose mass values can be aligned as 'mass ladders' to provide sequence information and to localize possible post-translational modifications. The most common dissociation method involves slow heating of even-electron (M+nH) n+ ions from electrospray ionization by ...
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The chemistry of disulfide exchange in biological systems is well studied. However, very little information is available concerning the actual origin of disulfide bonds. Here we show that DsbB, a protein required for disulfide bond formation in vivo, uses the oxidizing power of quinones to generate disulfides de novo. This is a novel catalytic activity, which to our knowledge has not yet been d...
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Most proteins in nature are chemically modified after they are made to control how, when, and where they function. The 3 core features of proteins are posttranslationally modified: amino acid side chains can be modified, peptide bonds can be cleaved or isomerized, and disulfide bonds can be cleaved. Cleavage of peptide bonds is a major mechanism of protein control in the circulation, as exempli...
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Disulfide bonds play an important role in the structural stability of the proteins that contain them. Yet, little is known about the specificity with which they are formed. To address this, a representative set of disulfide bonds from nonhomologous eukaryotic polypeptides was created. The amino acid sequences flanking these disulfide bonds were searched for conserved patterns that may reflect r...
متن کاملAntibody scFv fragments without disulfide bonds made by molecular evolution.
We generated stable and functional cysteine-free antibody single-chain fragments (scFv) lacking the conserved disulfide bonds in both VH and VL. This was achieved by molecular evolution, starting from the scFv fragment of the levan binding antibody ABPC48, which is naturally missing one of the conserved cysteine residues, by using DNA shuffling and phage display. Several of the selected sequenc...
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ژورنال
عنوان ژورنال: The Journal of Physical Chemistry A
سال: 2001
ISSN: 1089-5639,1520-5215
DOI: 10.1021/jp0040603