Quasielastic light scattering studies of polypeptides: evidence for chain extension in solution

Authors : Bahattin M BAYSAL, Çiğdem KARADAĞ

Pages : 480-491

Doi:10.3906/kim-1301-11

View : 18 | Download : 8

Publication Date : 0000-00-00

Article Type : Research Paper

Abstract :Dynamic light scattering and viscosimetric methods were used to study polypeptides including polyleucine, poly insert ignore into journalissuearticles values(g-benzyl-L-glutamate);, poly insert ignore into journalissuearticles values(a-L-glutamic acid);, and polyproline II. Chain extension showing rod-like and flexible conformations occurred in polyinsert ignore into journalissuearticles values(g -benzyl-L-glutamate); and polyproline II solutions as these solutions were diluted in glacial acetic acid or in a mixed solvent of acetic acid and dichloromethane. The elongation of chains in polyinsert ignore into journalissuearticles values(g -benzyl-L-glutamate); and polyproline II solutions was studied by dynamic light scattering and viscosimetric methods. This nonenzymatic growth of peptide chains provides data on primordial synthesis of protein molecules in the absence of cell machinery and for this reason these reactions may yield valuable data for further studies.
Keywords : Polypeptides, poly g benzyl L glutamate, polyproline II, dynamic light scattering, hydrodynamic radius, intrinsic viscosity, chain extension