Sampling of Protein Dynamics in Nanosecond Time Scale by15N NMR Relaxation and Self-Diffusion Measurements

1999 ◽  
Vol 17 (1) ◽  
pp. 157-174 ◽  
Author(s):  
Vladislav Yu. Orekhov ◽  
Dmitry M. Korzhnev ◽  
Konstantine V. Pervushin ◽  
Eberhard Hoffmann ◽  
Alexander S. Arseniev
Keyword(s):  
Protein Dynamics ◽  
Time Scale ◽  
Nmr Relaxation ◽  
Self Diffusion ◽  
Nanosecond Time Scale

scholarly journals Prion protein dynamics before aggregation

2017 ◽  
Vol 114 (14) ◽  
pp. 3572-3577 ◽  
Author(s):  
Kinshuk Raj Srivastava ◽  
Lisa J. Lapidus
Keyword(s):  
Protein Dynamics ◽  
Neurodegenerative Disorders ◽  
Syrian Hamster ◽  
Time Scale ◽  
Molecular Basis ◽  
Prion Proteins ◽  
Prion Diseases ◽  
Hydrophobic Residues ◽  
Protein Deposits ◽  
Polypeptide Backbone

Prion diseases, like Alzheimer’s disease and Parkinson disease, are rapidly progressive neurodegenerative disorders caused by misfolding followed by aggregation and accumulation of protein deposits in neuronal cells. Here we measure intramolecular polypeptide backbone reconfiguration as a way to understand the molecular basis of prion aggregation. Our hypothesis is that when reconfiguration is either much faster or much slower than bimolecular diffusion, biomolecular association is not stable, but as the reconfiguration rate becomes similar to the rate of biomolecular diffusion, the association is more stable and subsequent aggregation is faster. Using the technique of Trp–Cys contact quenching, we investigate the effects of various conditions on reconfiguration dynamics of the Syrian hamster and rabbit prion proteins. This protein exhibits behavior in all three reconfiguration regimes. We conclude that the hamster prion is prone to aggregation at pH 4.4 because its reconfiguration rate is slow enough to expose hydrophobic residues on the same time scale that bimolecular association occurs, whereas the rabbit sequence avoids aggregation by reconfiguring 10 times faster than the hamster sequence.

scholarly journals Characterization of Internal Protein Dynamics and Conformational Entropy by NMR Relaxation

2019 ◽  
pp. 237-284 ◽  
Author(s):  
Matthew A. Stetz ◽  
José A. Caro ◽  
Sravya Kotaru ◽  
Xuejun Yao ◽  
Bryan S. Marques ◽  
...  
Keyword(s):  
Protein Dynamics ◽  
Nmr Relaxation ◽  
Conformational Entropy ◽  
Internal Protein

scholarly journals Nanometer-sized dynamic entities in an aqueous system

2015 ◽  
Vol 17 (6) ◽  
pp. 4466-4471 ◽  
Author(s):  
E. Mamontov ◽  
P. Zolnierczuk ◽  
M. Ohl
Keyword(s):  
Time Scale ◽  
Aqueous System ◽  
Slow Relaxation ◽  
Nanosecond Time Scale ◽  
System P

A slow relaxation in an aqueous system is associated with nanometer-sized entities with a lifetime on nanosecond time scale.

Ultrafast Terahertz Photoconductivity of Bulk Heterojunction Materials Reveals High Carrier Mobility up to Nanosecond Time Scale

2012 ◽  
Vol 134 (29) ◽  
pp. 11836-11839 ◽  
Author(s):  
Carlito S. Ponseca ◽  
Arkady Yartsev ◽  
Ergang Wang ◽  
Mats R. Andersson ◽  
Dimali Vithanage ◽  
...  
Keyword(s):  
Time Scale ◽  
Carrier Mobility ◽  
Bulk Heterojunction ◽  
Nanosecond Time Scale ◽  
High Carrier Mobility ◽  
High Carrier
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