New Insight into the Wax Precipitation Process: In Situ NMR Imaging Study in a Cold Finger Cell

2016 ◽  
Vol 30 (11) ◽  
pp. 9003-9013 ◽  
Author(s):  
Evgeny V. Morozov ◽  
Oleg V. Falaleev ◽  
Oleg N. Martyanov
Fuel ◽  
2000 ◽  
Vol 79 (3-4) ◽  
pp. 405-416 ◽  
Author(s):  
K Saito ◽  
I Komaki ◽  
K.-I Hasegawa ◽  
H Tsuno

1998 ◽  
Vol 102 (17) ◽  
pp. 3090-3098 ◽  
Author(s):  
Igor V. Koptyug ◽  
Vladimir B. Fenelonov ◽  
Ludmila Yu. Khitrina ◽  
Renad Z. Sagdeev ◽  
Valentin N. Parmon

2013 ◽  
Vol 135 (50) ◽  
pp. 18968-18980 ◽  
Author(s):  
Hao Wang ◽  
Alexander C. Forse ◽  
John M. Griffin ◽  
Nicole M. Trease ◽  
Lorie Trognko ◽  
...  

2015 ◽  
Vol 119 (37) ◽  
pp. 12238-12248 ◽  
Author(s):  
Athinthra Krishnaswamy Sethurajan ◽  
Sergey A. Krachkovskiy ◽  
Ion C. Halalay ◽  
Gillian R. Goward ◽  
Bartosz Protas

2020 ◽  
Vol 92 (10) ◽  
pp. 1575-1583
Author(s):  
Emiko Okamura ◽  
Kenzo Aki

AbstractIn-situ analytical methods are essential for the reliable observation of peptide reactions without perturbation of the system. In this work, a real-time in-situ NMR analysis was performed to gain insight into the initial stage of the aggregation of amyloid-beta (Aβ) 8–25 monomers, S8GY10EVHHQKLVFF20AEDVG25, in solution prior to the fibril formation. NMR chemical shift and intensity changes in combination with the CD spectra revealed no changes in Aβ secondary structure, but the presence of soluble, oligomeric intermediates followed by the appearance of insoluble and non-structured aggregates before β-fibril formation. Molecular views of intermediates and aggregation mechanisms were proposed in comparison with NMR spectral changes in wild-type Aβ 8–25 and its two mutants, A21G and E22G. The mutation of just one amino acid modified the aggregation properties of Aβ 8–25; it slowed or accelerated the fibril formation by controlling the progress of conversion from monomer to aggregate via a soluble, small oligomer.


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