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Functional Dissection of the Proton Pumping Modules of Mitochondrial Complex I
A catalytically active subcomplex of respiratory chain complex I lacks 14 of its 42 subunits yet retains half of its proton-pumping capacity, indicating that its membrane arm has two pump modules.
A scaffold of accessory subunits links the peripheral arm and the distal proton-pumping module of mitochondrial complex I.
TLDR
A model is derived for the arrangement of the subunits in the membrane arm of mitochondrial complex I from the aerobic yeast Yarrowia lipolytica and biochemical evidence on the assignment of individual subunits to the subdomains of complex I and sequence-based predictions for the targeting of sub units to different mitochondrial compartments.
Oligomeric structure of ExbB and ExbB-ExbD isolated from Escherichia coli as revealed by LILBID mass spectrometry.
TLDR
Using laser-induced liquid bead ion desorption mass spectrometry (LILBID-MS), the oligomeric structure of ExbB was determined to be mainly hexameric (ExbB(6), with minor amounts of trimeric, dimeric, and monomeric oligomers, and the final complex including TonB is assembled.
The influence of densely organized maltose shells on the biological properties of poly(propylene imine) dendrimers: new effects dependent on hydrogen bonding.
TLDR
Improved improvements will initiate the development of the next platform of glycodendrimers in which apparently contrary properties can be combined, and this will enable, for example, therapeutic products such as more efficient and less toxic antiamyloid agents to be synthesized.
Subunit mass fingerprinting of mitochondrial complex I.
A tridecameric c ring of the adenosine triphosphate (ATP) synthase from the thermoalkaliphilic Bacillus sp. strain TA2.A1 facilitates ATP synthesis at low electrochemical proton potential
TLDR
The operation of a c ring with 13 subunits renders the thermodynamic problem of ATP synthesis at alkaline pH less severe and may represent a strategy for ATP synthesizing at low electrochemical potential.
Three-dimensional Structure of A1A0 ATP Synthase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Electron Microscopy*
TLDR
The archaeal ATP synthase is a multisubunit complex that consists of a catalytic A1 part and a transmembrane, ion translocation domain A0, which was isolated from the hyperthermophile Pyrococcus furiosus by laser-induced liquid bead ion desorption.
Dimerization of human 5-lipoxygenase
TLDR
Human 5-lipoxygenase can form dimers as shown here via native gel electrophoresis, gel filtration chromatography and LILBID (laser induced liquid bead ion desorption) mass spectrometry, which suggests a head to tail orientation of the dimer which explains the localization of previously reported ATP binding sites.
Influence of surface groups on poly(propylene imine) dendrimers antiprion activity.
TLDR
A new working model is proposed which proposes dendrimers eliminate PrP(Sc) by destabilizing the protein and rendering it susceptible to proteolysis, which is not dependent on any particular charge of d endrimer, but does require a high density of reactive surface groups.
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