Small angle neutron scattering studies on protein denaturation induced by different methods

Pramana

A G Wagh¹  S Chodankar1¹  J Kohlbrecher²  V K Aswal¹  R Vavrin² 

[1] Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai 400 085, India$$;Laboratory for Neutron Scattering, ETH Zurich & Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland$$

关键词: Protein denaturation;    gelation and unfolding of protein;    small angle neutron scattering.;   

DOI  :  

学科分类：物理（综合）

来源: Indian Academy of Sciences

【 摘 要 】

Small angle neutron scattering (SANS) has been used to study conformational changes in protein bovine serum albumin (BSA) as induced by varying temperature and in the presence of protein denaturating agents urea and surfactant. BSA has pro-late ellipsoidal shape and is found to be stable up to 60°C above which it denaturates and subsequently leads to aggregation. The protein solution exhibits a fractal structure at temperatures above 64°C, with fractal dimension increasing with temperature. BSA protein is found to unfold in the presence of urea at concentrations greater than 4 M and acquires a random coil Gaussian chain conformation. The conformation of the unfolded protein in the presence of surfactant has been determined directly using contrast variation SANS measurements by contrast matching surfactant molecules. The protein acquires a random coil Gaussian conformation on unfolding with its radius of gyration increasing with increase in surfactant concentration

【 授权许可】

Unknown