Apocytochrome b5 with a typical heme-binding motif of HPGG, and its variants with mutated motifs, GPGG, GPGH, HVGG, and HPGP, have been subjected to molecular dynamics simulation. Comparison of the dynamic consequence...Apocytochrome b5 with a typical heme-binding motif of HPGG, and its variants with mutated motifs, GPGG, GPGH, HVGG, and HPGP, have been subjected to molecular dynamics simulation. Comparison of the dynamic consequences has revealed the crucial role of HPGG in assembling the heine group of cytochrome b5 and in modulating protein structure, property and function.展开更多
In contrast to the horse heart apocytochrome c,the chicken heart apocytochrome c under-went a conformational change from random coil to partial folding during a renaturation process.When theapocytochrome horse heart a...In contrast to the horse heart apocytochrome c,the chicken heart apocytochrome c under-went a conformational change from random coil to partial folding during a renaturation process.When theapocytochrome horse heart and that of chicken heart c were subjected to a translocation assay in vitro usinglarge trypsin-enclosed unilamellar vesicles from soybean phospholipids,the ability of the chicken heart apoc-ytochrome c to penetrate into the liposomes was found to decrease markedly with the renaturation procedure,while that of horse heart apocytochrome c remained relatively constant.Observations from circular dichroismmeasurement on the induction of secondary folding of these two species of apocytochrome c upon interactionwith soybean phospholipid vesicles suggested that a more flexible structure of apocytochrome c embedded inthe lipid matrix be required for its efficient translocation across the bilayer.展开更多
The dependence of import of chicken heart apocytochrome c on its transformation to holoform by heme attachment was studied. Results showed that there was no difference in the translocation of apocytochrome c across th...The dependence of import of chicken heart apocytochrome c on its transformation to holoform by heme attachment was studied. Results showed that there was no difference in the translocation of apocytochrome c across the mitochondrial membrane in the presence or absence of hemin + dithionite. Furthermore, two heme unattached mutants (H18D, C17S) were prepared, which could still be accumulated in mitochondria, but their import velocity was obviously reduced.展开更多
Chicken heart apocytochrome c has been shown to exhibit much stronger foldingpropensity than those from other species, and its partially-folding and aggregation havebeen studied in detail, with the partially-folded st...Chicken heart apocytochrome c has been shown to exhibit much stronger foldingpropensity than those from other species, and its partially-folding and aggregation havebeen studied in detail, with the partially-folded state possessing some characteristics offolding intermediate. It contains a substantial fraction of secondary structure, with de-展开更多
基金supported by the initial foundation for Ph.D.introduced into University of South China(No.506XJQ06001).
文摘Apocytochrome b5 with a typical heme-binding motif of HPGG, and its variants with mutated motifs, GPGG, GPGH, HVGG, and HPGP, have been subjected to molecular dynamics simulation. Comparison of the dynamic consequences has revealed the crucial role of HPGG in assembling the heine group of cytochrome b5 and in modulating protein structure, property and function.
基金the National Natural Science Foundation of China
文摘In contrast to the horse heart apocytochrome c,the chicken heart apocytochrome c under-went a conformational change from random coil to partial folding during a renaturation process.When theapocytochrome horse heart and that of chicken heart c were subjected to a translocation assay in vitro usinglarge trypsin-enclosed unilamellar vesicles from soybean phospholipids,the ability of the chicken heart apoc-ytochrome c to penetrate into the liposomes was found to decrease markedly with the renaturation procedure,while that of horse heart apocytochrome c remained relatively constant.Observations from circular dichroismmeasurement on the induction of secondary folding of these two species of apocytochrome c upon interactionwith soybean phospholipid vesicles suggested that a more flexible structure of apocytochrome c embedded inthe lipid matrix be required for its efficient translocation across the bilayer.
基金Project supported by the National Natural Science Foundation of China (Grant No. 39730130).
文摘The dependence of import of chicken heart apocytochrome c on its transformation to holoform by heme attachment was studied. Results showed that there was no difference in the translocation of apocytochrome c across the mitochondrial membrane in the presence or absence of hemin + dithionite. Furthermore, two heme unattached mutants (H18D, C17S) were prepared, which could still be accumulated in mitochondria, but their import velocity was obviously reduced.
文摘Chicken heart apocytochrome c has been shown to exhibit much stronger foldingpropensity than those from other species, and its partially-folding and aggregation havebeen studied in detail, with the partially-folded state possessing some characteristics offolding intermediate. It contains a substantial fraction of secondary structure, with de-
