The study of amorphous aggregation of tobacco mosaic virus coat protein by dynamic light scattering

Mechanism of suppression of dithiothreitol-induced aggregation of bovine α-lactalbumin by α-crystallin

“…Analogous mechanism of protein aggregation involving the stage of formation of the start aggregates and the stage of sticking of the start aggregates and the aggregates of higher order was proposed for thermal aggregation of proteins in our previous works [1][2][3]5,7,8]. In the case of DTT-induced aggregation of α-lactalbumin the size of the start aggregates remains practically unchangeable at the variation of the α-lactalbumin concentration.…”

“…The higher the 1/t 2R value, the higher is the rate of aggregation. Analysis of the full dependences of R h of the protein aggregates for thermal aggregation of Phb on time [1,3,[5][6][7][8] showed that above the definite point of time designated as t ⁎ the dependences of R h on time followed the power law:…”

“…The hydrodynamic radius of the start aggregates was tens of nanometers. The start aggregate formation was revealed in the process of thermal aggregation of the following model substrates: β L -crystallin from bovine lens [1], glyceraldehyde-3-phosphate dehydrogenase and glycogen phosphorylase b from rabbit skeletal muscle [2][3][4][5][6], aspartate aminotransferase from pig heart mitochondria [7] and tobacco mosaic virus coat protein [8].…”

Single-molecule Analyses of the Dynamics of Heat Shock Protein 104 (Hsp104) and Protein Aggregates

“…At first, we conducted DLS experiments to characterize the luciferase aggregates. DLS is a particle size analysis method applicable to protein aggregates (33,34). The DLS measurements revealed that the luciferase aggregates at the initial stage had a heterogeneous size distribution (Fig.…”

Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle: Mechanism of protective action of α‐crystallin

“…According to Nicolai and coworkers, [41][42][43][44][45] thermal aggregation of b-lactoglobulin at pH 7 in the presence of 0.1M NaCl proceeds through the stage of the formation of the primary aggregates containing about 100 denatured monomers. In the works by Kurganov and coworkers, 5,23,24,46 these primary aggregates were called the start aggregates to stress the circumstance that the further growth of the primary aggregates occur by their sticking but not by the attachment of the individual molecules of denatured protein. The sticking of the start aggregates and aggregates of higher order results finally in the formation of the large-sized aggregates prone to precipitation.…”