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A high-precision solution structure of the C-terminal minicollagen cysteine rich domain of Hydra has been determined using modern heteronuclear and weak alignment NMR techniques at natural isotope abundance. The domain consists of only 24 amino acids, six of which are prolines and six are cysteines bonded in disulfide bridges that constrain the structure into a new fold. The redox equilibrium of the structure has been characterized from a titration with glutathione. No local native structures are detectable in the reduced form. Thus, oxidation and folding are tightly coupled.
Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation.,Meier S, Haussinger D, Pokidysheva E, Bachinger HP, Grzesiek S FEBS Lett. 2004 Jul 2;569(1-3):112-6. PMID:15225618[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Meier S, Haussinger D, Pokidysheva E, Bachinger HP, Grzesiek S. Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation. FEBS Lett. 2004 Jul 2;569(1-3):112-6. PMID:15225618 doi:10.1016/j.febslet.2004.05.034
