Coupling effects of thiol and urea-type groups for promotion of oxidative protein folding.
Sign Up to like & getrecommendations! Published in 2019 at "Chemical communications"
DOI: 10.1039/c8cc08657e
Abstract: Coupling of thiol and urea-type -NHC([double bond, length as m-dash]X)NH2 (X = O or NH) groups is effective in promoting oxidative protein folding. In particular, a thiol compound coupled with a guanidyl (X = NH)… read more here.
Keywords: protein folding; thiol urea; urea type; oxidative protein ... See more keywords
A cryptic oxidoreductase safeguards oxidative protein folding in Corynebacterium diphtheriae
Sign Up to like & getrecommendations! Published in 2023 at "Proceedings of the National Academy of Sciences of the United States of America"
DOI: 10.1073/pnas.2208675120
Abstract: Significance Oxidative protein folding via disulfide bond formation is an important process in bacteria, although it can be dispensable in various organisms. In many gram-positive Actinobacteria, deletion of mdbA coding for the conserved thiol-disulfide oxidoreductase… read more here.
Keywords: oxidoreductase; protein folding; corynebacterium diphtheriae; oxidative protein ... See more keywords