AFM Study of Temperature and pH Effects on BSA Structure and Adhesion
作者： Mengyi Hao , Yulin Ji , Yujuan Wang , Yunfei Chen
DOI: 10.1109/3M-NANO46308.2019.8947371
关键词: Atomic force microscopy 、 Chemistry 、 Bovine serum albumin 、 Protein structure 、 Adhesion 、 Silicon 、 Magazine 、 Biophysics 、 Molecule 、 Spatial structure
摘要: With the wide application of biomacromolecular materials such as proteins, it is increasingly important to explore influence external environment on protein structure and properties. In this paper, effects temperature pH adhesion bovine serum albumin (BSA) were studied by atomic force microscopy (AFM). The experimental results showed that spatial changed gradually with increase temperature, which was manifested a decrease in height molecule. diversification BSA measured. And between silicon tips decreased when increased. By varying environment, found molecule reduced under strong acidic or alkaline conditions, accompanied adhesion. Temperature are revealed be effective factors transforming protein, besides affecting mechanical properties protein.
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