Journal Article10.1016/J.JMB.2005.07.033
Kinetically Controlled Thermal Response of β2-Microglobulin Amyloid Fibrils
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TL;DR: It is suggested that the heating rate-dependent negative change in heat capacity is coupled to the association of amyloid fibrils with characteristic hydration pattern.
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About: This article is published in Journal of Molecular Biology. The article was published on 23 Sep 2005. The article focuses on the topics: Amyloid beta & Fibril.
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Citations
The Natively Unfolded Character of Tau and Its Aggregation to Alzheimer-like Paired Helical Filaments†
TL;DR: It is shown that soluble Tau remains natively unfolded even when its net charge is minimized, in contrast to other unfolded proteins, suggesting that the lack of hydrophobic residues but not the net charge accounts for unfolded nature of soluble Tau.
276
Inhibiting, promoting, and preserving stability of functional protein fibrils
Owen G. Jones,Raffaele Mezzenga +1 more
TL;DR: While various strategies are presented on the breakdown of mature protein fibrils, emphasis is given to the approaches leading to increased rigidity and length of resultant fibril.
134
The thermodynamic stability of amyloid fibrils studied by differential scanning calorimetry.
TL;DR: This work analyzed the thermal melting of the amyloid fibrils of the N47A mutant of the alpha-spectrin SH3 domain by differential scanning calorimetry (DSC) and found that with the use of appropriate models of analysis DSC has an extraordinary potential to analyze the thermodynamic determinants of amyloids fibril stability.
89
Heat of supersaturation-limited amyloid burst directly monitored by isothermal titration calorimetry
Tatsuya Ikenoue,Young-Ho Lee,József Kardos,Hisashi Yagi,Takahisa Ikegami,Hironobu Naiki,Yuji Goto +6 more
TL;DR: Direct heat measurements of the formation of amyloid fibrils are established using isothermal titration calorimetry (ITC), and the thermodynamic parameters of fibrillation obtained under various protein concentrations and temperatures were consistent with the main-chain dominated structural model of fbrils, in which overall packing was less than that of the native structures.
83
Water Molecular System Dynamics Associated with Amyloidogenic Nucleation as Revealed by Real Time Near Infrared Spectroscopy and Aquaphotomics
TL;DR: Near infrared (NIR) spectral monitoring of water structural changes in real time during the nucleation-dependent fibrillation of insulin found characteristic transformations of water structure have been detected and could be used further as a biomarker for early non-invasive diagnosis of amyloidoses prior to explosive amplification and deposits ofAmyloid fibrils.
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References
The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation.
TL;DR: It is firmly established that amyloid formation and protein folding represent two fundamentally different ways of organizing polypeptides into ordered conformations.
Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin
TL;DR: It is shown that the proposed model may be considered as being one particular case of that proposed by Lumry and Eyring, where N in equilibrium D----I is the native state, D the unfolded one, and I a final state, irreversibly arrived at from D.
455
Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro
Hironobu Naiki,Norikazu Hashimoto,Satoru Suzuki,Hideki Kimura,Kazuya Nakakuki,Fumitake Gejyo +5 more
TL;DR: Quantitative fiuorometry revealed that extension of fAβ2M proceeded by a pseudo-first order exponential increase as measured by the fluorescence of ThT, which is essential to build up a kinetic experimental system to analyze fA β2M formation in vitro.
218
Hierarchical Assembly of β2-Microglobulin Amyloid In Vitro Revealed by Atomic Force Microscopy
TL;DR: The kinetics of spontaneous assembly of amyloid fibrils of wild-type beta(2)-microglobulin (beta(2)M) in vitro, under acid conditions and low ionic strength, has been followed using thioflavin-T (ThT) binding.
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