The effects of denaturants on protein conformation and behavior at air/solution interface

Su Hwa Chang, Liang Yu Chen, Wen Yih Chen

研究成果: 雜誌貢獻期刊論文同行評審

13 引文 斯高帕斯(Scopus)

摘要

In this study, we discuss the interfacial behavior of five proteins with different conformational character, and each is investigated in native and denatured states. The protein molecules are layered and spread onto the air/solution interfaces to form protein monolayer. The surface pressure-time (Π(t)) and surface pressure-area per molecule (Π-A) isotherms were measured by using the Langmuir-Blodgett (LB) balance consisted of a Nima trough system. The differences between monolayered protein's behaviors at air/solution interface indicate that denaturants, such as urea, guanidinium chloride and dithiothreitol, have different effects on conformational changes of proteins. Additionally, the interfacial behavior of the proteins in our study provides a fundamental profile about the protein structural stability and implies industrial applications in protein refolding process.

原文???core.languages.en_GB???
頁(從 - 到)1-6
頁數6
期刊Colloids and Surfaces B: Biointerfaces
41
發行號1
DOIs
出版狀態已出版 - 10 3月 2005

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