scholarly journals Dynamics of the disordered N-terminal domain of amyloid-β(1-40) fibrils using deuterium solid-state NMR, application to wild-type Aβ, β-bend mutants, and post-translational modifications

2020 ◽  
Author(s):  
Liliya Vugmeyster
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Β ◽  
Wild Type ◽  
Post Translational Modifications ◽  
Terminal Domain

scholarly journals Structural characteristics of oligomers formed by pyroglutamate-modified amyloid β peptides studied by solid-state NMR

2020 ◽  
Vol 22 (29) ◽  
pp. 16887-16895 ◽  
Author(s):  
Holger A. Scheidt ◽  
Anirban Das ◽  
Alexander Korn ◽  
Martin Krueger ◽  
Sudipta Maiti ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Structural Characteristics ◽  
Amyloid Β ◽  
Wild Type

Structure of oligomers of truncated and pyroglutamate modified amyloid β variants is similar to the wild type.

scholarly journals Solid-State NMR Reveals Structural Differences between Fibrils of Wild-Type and Disease-Related A53T Mutant α-Synuclein

2008 ◽  
Vol 380 (3) ◽  
pp. 444-450 ◽  
Author(s):  
Henrike Heise ◽  
M. Soledad Celej ◽  
Stefan Becker ◽  
Dietmar Riedel ◽  
Avishay Pelah ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Wild Type ◽  
Structural Differences

scholarly journals Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR

2020 ◽  
Vol 117 (13) ◽  
pp. 7171-7175
Author(s):  
Zhiyu Sun ◽  
Yunyao Xu ◽  
Dongyu Zhang ◽  
Ann E. McDermott
Keyword(s):  
Solid State ◽  
Binding Affinity ◽  
Solid State Nmr ◽  
Selectivity Filter ◽  
Wild Type ◽  
Proton Binding ◽  
Allosteric Coupling ◽  
Neutral Ph ◽  
Potassium Channel Kcsa ◽  
Potassium Binding

Transmembrane allosteric coupling is a feature of many critical biological signaling events. Here we test whether transmembrane allosteric coupling controls the potassium binding affinity of the prototypical potassium channel KcsA in the context of C-type inactivation. Activation of KcsA is initiated by proton binding to the pH gate upon an intracellular drop in pH. Numerous studies have suggested that this proton binding also prompts a conformational switch, leading to a loss of affinity for potassium ions at the selectivity filter and therefore to channel inactivation. We tested this mechanism for inactivation using a KcsA mutant (H25R/E118A) that exhibits an open pH gate across a broad range of pH values. We present solid-state NMR measurements of this open mutant at neutral pH to probe the affinity for potassium at the selectivity filter. The potassium binding affinity in the selectivity filter of this mutant, 81 mM, is about four orders of magnitude weaker than that of wild-type KcsA at neutral pH and is comparable to the value for wild-type KcsA at low pH (pH ≈ 3.5). This result strongly supports our assertion that the open pH gate allosterically affects the potassium binding affinity of the selectivity filter. In this mutant, the protonation state of a glutamate residue (E120) in the pH sensor is sensitive to potassium binding, suggesting that this mutant also has flexibility in the activation gate and is subject to transmembrane allostery.

scholarly journals Solid-state NMR sequential assignment of an Amyloid-β(1–42) fibril polymorph

2016 ◽  
Vol 10 (2) ◽  
pp. 269-276 ◽  
Author(s):  
Francesco Ravotti ◽  
Marielle Aulikki Wälti ◽  
Peter Güntert ◽  
Roland Riek ◽  
Anja Böckmann ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Β ◽  
Sequential Assignment

scholarly journals Solid-state NMR Reveals a Close Structural Relationship between Amyloid-β Protofibrils and Oligomers

2012 ◽  
Vol 287 (27) ◽  
pp. 22822-22826 ◽  
Author(s):  
Holger A. Scheidt ◽  
Isabel Morgado ◽  
Daniel Huster
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Β ◽  
Structural Relationship

Association of amyloid-β peptide with membrane surfaces monitored by solid state NMR

2002 ◽  
Vol 4 (22) ◽  
pp. 5524-5530 ◽  
Author(s):  
Fredrick Lindström ◽  
Marcus Bokvist ◽  
Tobias Sparrman ◽  
Gerhard Gröbner
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Membrane Surfaces

scholarly journals Solid-state NMR sequential assignments of the N-terminal domain of HpDnaB helicase

2015 ◽  
Vol 10 (1) ◽  
pp. 13-23 ◽  
Author(s):  
Thomas Wiegand ◽  
Carole Gardiennet ◽  
Francesco Ravotti ◽  
Alexandre Bazin ◽  
Britta Kunert ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Terminal Domain
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