The Macromolecular Organization of Cellulose and Chitin

1982 ◽  
pp. 403-428 ◽  
Author(s):  
John Blackwell
Keyword(s):  
Macromolecular Organization

scholarly journals Molecular characterization of a complex of apoptosis-inducing factor 1 with cytochrome c oxidase of the mitochondrial respiratory chain

2021 ◽  
Vol 118 (39) ◽  
pp. e2106950118
Author(s):  
Johannes F. Hevler ◽  
Riccardo Zenezeni Chiozzi ◽  
Alfredo Cabrera-Orefice ◽  
Ulrich Brandt ◽  
Susanne Arnold ◽  
...  
Keyword(s):  
Oxidative Phosphorylation ◽  
Respiratory Chain ◽  
Structural Model ◽  
Direct Electron Transfer ◽  
Mitochondrial Respiratory Chain ◽  
Structural Restraints ◽  
Apoptosis Inducing Factor ◽  
Insight Into ◽  
Macromolecular Organization

Combining mass spectrometry–based chemical cross-linking and complexome profiling, we analyzed the interactome of heart mitochondria. We focused on complexes of oxidative phosphorylation and found that dimeric apoptosis-inducing factor 1 (AIFM1) forms a defined complex with ∼10% of monomeric cytochrome c oxidase (COX) but hardly interacts with respiratory chain supercomplexes. Multiple AIFM1 intercross-links engaging six different COX subunits provided structural restraints to build a detailed atomic model of the COX-AIFM12 complex (PDBDEV_00000092). An application of two complementary proteomic approaches thus provided unexpected insight into the macromolecular organization of the mitochondrial complexome. Our structural model excludes direct electron transfer between AIFM1 and COX. Notably, however, the binding site of cytochrome c remains accessible, allowing formation of a ternary complex. The discovery of the previously overlooked COX-AIFM12 complex and clues provided by the structural model hint at potential roles of AIFM1 in oxidative phosphorylation biogenesis and in programmed cell death.

Macromolecular organization of natural and recombinant lung surfactant protein SP 28–36

1988 ◽  
Vol 201 (1) ◽  
pp. 219-227 ◽  
Author(s):  
Tilman Voss ◽  
Harald Eistetter ◽  
Klaus P. Schäfer ◽  
Jürgen Engel
Keyword(s):  
Lung Surfactant ◽  
Surfactant Protein ◽  
Lung Surfactant Protein ◽  
Macromolecular Organization

Determining the geometry of oligomers of the human epidermal growth factor family on cells with <10 nm resolution

2015 ◽  
Vol 43 (3) ◽  
pp. 309-314 ◽  
Author(s):  
Sarah R. Needham ◽  
Laura C. Zanetti-Domingues ◽  
Kathrin M. Scherer ◽  
Michael Hirsch ◽  
Daniel J. Rolfe ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Spatial Resolution ◽  
Single Molecule ◽  
Egf Receptor ◽  
Limited Range ◽  
Length Scales ◽  
Human Epidermal Growth Factor ◽  
Epidermal Growth ◽  
Macromolecular Organization

There is a limited range of methods available to characterize macromolecular organization in cells on length scales from 5–50 nm. We review methods currently available and show the latest results from a new single-molecule localization-based method, fluorophore localization imaging with photobleaching (FLImP), using the epidermal growth factor (EGF) receptor (EGFR) as an example system. Our measurements show that FLImP is capable of achieving spatial resolution in the order of 6 nm.

Structure and Macromolecular Organization of Type VI Collagen

1985 ◽  
Vol 460 (1 Biology, Chem) ◽  
pp. 25-37 ◽  
Author(s):  
JÜRGEN ENGEL ◽  
HEINZ FURTHMAYR ◽  
ERICH ODERMATT ◽  
HELGA MARK ◽  
MONIQUE AUMAILLEY ◽  
...  
Keyword(s):  
Type Vi Collagen ◽  
Macromolecular Organization
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