A comparative study of fibrillation kinetics of two homologous proteins under identical solution condition

The physical basis of fabrication of amyloid-based hydrogels by lysozyme

“…The ball drop time (BDT), the time of travel of the ball between two points through the samples, and RLS values provide information about the rheological (ow) properties and aggregation of the protein, respectively. 17,18,33 The transitions monitored by BDT and RLS were found not to be superimposable, when normalised to the gel fraction (f gel ) and the aggregate fraction (f scat ) (Fig. 3C).…”

“…To examine the refolding process, samples were cooled from 90 C to 25 C. The process of unfolding and refolding was monitored using intrinsic uorescence, far-UV CD and ANS uorescence as previously described by our group. 17,20 The resulting transition curves were also analysed to calculate the T m of unfolding/refolding reactions as previously described by our group. 17,20 3.…”

“…17,20 The resulting transition curves were also analysed to calculate the T m of unfolding/refolding reactions as previously described by our group. 17,20 3. Results…”

“…17,19,30,31 ThT and CR interact with the cross-b motif and give information about the secondary structure of the samples. 17,19,31,32 The ThT uorescence and CR difference spectra analyses showed a marked ability of the hydrogel to interact with these dyes and cause the spectral changes associated with amyloid brils. The high content of b-sheet structures observed in the HCM is in agreement with the ability of the same samples to bind amyloiddiagnostic dyes, which suggests that such b-sheet structures are mainly intermolecular.…”

Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins

“…Stabilization of native α‐helices of sequences with high fibrillation propensity in the partially unfolded state decelerates AF formation. The stabilization of α‐helices in nonamylogenic sequences can probably accelerate fibril formation of globular proteins (Chaudhary, Vispute, Shukla, & Ahmad, ). X‐ray diffraction patterns with reflections at 4.7, 9.7, and 12.6 Å have confirmed the amyloid nature of the fibrillar structures obtained by heating LYS solutions at pH 2.0 (Krebs et al., ).…”