Identification of Protein Folding Patterns Using Site-Directed Spin Labeling. Structural Characterization of a β-Sheet and Putative Substrate Binding Regions in the Conserved Domain of αA-Crystallin†

Biochemistry ◽  
1998 ◽  
Vol 37 (37) ◽  
pp. 12681-12688 ◽  
Author(s):  
Hanane A. Koteiche ◽  
Anderee R. Berengian ◽  
Hassane S. Mchaourab
Keyword(s):  
Protein Folding ◽  
Structural Characterization ◽  
Substrate Binding ◽  
Spin Labeling ◽  
Conserved Domain ◽  
Binding Regions ◽  
Site Directed Spin Labeling ◽  
Β Sheet

scholarly journals Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation

2015 ◽  
Vol 112 (16) ◽  
pp. E1994-E2003 ◽  
Author(s):  
Serene W. Chen ◽  
Srdja Drakulic ◽  
Emma Deas ◽  
Myriam Ouberai ◽  
Francesco A. Aprile ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Self Assembly ◽  
Protein Misfolding ◽  
Amyloid Fibril ◽  
Amyloid Formation ◽  
Image Reconstruction Techniques ◽  
Cryo Electron Microscopy ◽  
Amyloid Oligomers ◽  
Β Sheet

We describe the isolation and detailed structural characterization of stable toxic oligomers of α-synuclein that have accumulated during the process of amyloid formation. Our approach has allowed us to identify distinct subgroups of oligomers and to probe their molecular architectures by using cryo-electron microscopy (cryoEM) image reconstruction techniques. Although the oligomers exist in a range of sizes, with different extents and nature of β-sheet content and exposed hydrophobicity, they all possess a hollow cylindrical architecture with similarities to certain types of amyloid fibril, suggesting that the accumulation of at least some forms of amyloid oligomers is likely to be a consequence of very slow rates of rearrangement of their β-sheet structures. Our findings reveal the inherent multiplicity of the process of protein misfolding and the key role the β-sheet geometry acquired in the early stages of the self-assembly process plays in dictating the kinetic stability and the pathological nature of individual oligomeric species.

scholarly journals Characterization of the Linker 2 Region in Human Vimentin Using Site-Directed Spin Labeling and Electron Paramagnetic Resonance†

Biochemistry ◽  
2006 ◽  
Vol 45 (39) ◽  
pp. 11737-11743 ◽  
Author(s):  
John F. Hess ◽  
Madhu S. Budamagunta ◽  
Rebecca L. Shipman ◽  
Paul G. FitzGerald ◽  
John C. Voss
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Spin Labeling ◽  
Paramagnetic Resonance ◽  
Site Directed Spin Labeling ◽  
Electron Paramagnetic

scholarly journals Identification of a α‐helical molten globule intermediate and structural characterization of β‐cardiotoxin, an all β‐sheet protein isolated from the venom ofOphiophagus hannah(king cobra)

2019 ◽  
Vol 28 (5) ◽  
pp. 952-963 ◽  
Author(s):  
Amrita Roy ◽  
Sun Qingxiang ◽  
Chapeaurouge Alex ◽  
Nandhakishore Rajagopalan ◽  
Chacko Jobichen ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Molten Globule ◽  
Β Sheet ◽  
King Cobra
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