Feige MJ, Hendershot LM. Disulfide bonds in ER protein folding and homeostasis. Curr Opin Cell Biol 2011;23:167-175.M.J. Feige, L.M. Hendershot, Disulfide bonds in ER protein folding and homeostasis, Curr. Opin. Cell. Biol. 23 (2011) 167-175....
bondsrefoldingrecombinantproteinsilkproteinWe constructed a gene encoding rCAS, recombinant constant and subrepeat protein, modeled after tandem repeats found in the major silk proteins synthesized by aquatic larvae of the midge, Chironomus tentans. Bacterially synthesized rCAS was purified to near ...
International Journal of Protein ResearchTamburro, A. M., Boccu, E., and Celotti, L., 1970, The role of disulfide bonds in the protein structure: Conformational studies on reduced ribonuclease and lysozyme, Int. J. Protein Res . 2 : 157....
SF Betz - 《Protein Science A Publication of the Protein Society》 被引量: 303发表: 2010年 Disulfide bonds in ER protein folding and homeostasis. Proteins that are expressed outside the cell must be synthesized, folded, and assembled in a way that ensures they can function in their designate...
We provide evidence that in vitro protein cross-linking can be accomplished in three concerted steps: (i) a change in protein conformation; (ii) formation of interchain disulfide bonds; and (iii) formation of interchain isopeptide cross-links. Oxidative refolding and thermal unfolding of ribonuclease...
The mechanism of regenerating the native disulfide bonds suggests an analogous scenario for conformational folding. Finally, engineered covalent cross-links may be used to assay for the association of protein segments in the folding transition state, as illustrated with RNase A. Show more...
In addition, Mia40 catalyzes the formation of disulfide bonds in anamorsin, a protein that has been implicated in Fe/S cluster assembly11. Beside the crucial role in mitochondrial protein structure, cysteine residues oxidation is important in the regulation of protein function within mitochondria. ...
Ignasiak3,*, Bun Chan4, Anna K. Croft5, Leo Radom4, Carl H. Schiesser6, David I. Pattison1,2 & Michael J. Davies1,2,3 Disulfide bonds play a key role in stabilizing protein structures, with disruption strongly associated with loss of protein function and ...
作者: A Kozik 摘要: All eight disulfide bonds in the apo-form of egg white riboflavin-binding protein were easily reduced by 2-mercaptoethanol and dithiothreitol. These bonds exhibited nearly the same reactivity, thus they appeared to be exposed in the native structure, or 'superficial'. The ...
Unlike other fatty acid-binding proteins, cutaneous (epidermal) fatty acid-binding proteins contain a large number of cysteine residues. The status of the five cysteine residues in rat cutaneous fatty acid-binding protein was examined by chemical and mass-spectrometric analyses. Two disulfide bonds we...