title: The effects of denaturants on protein conformation and behavior at air/solution interface.
abstract: 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 (Pi(t)) and surface pressure-area per molecule (Pi-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.
authors.affiliation: Department of Chemical and Material Engineering, National Central University, Chung-Li 320, Taiwan.
authors.forename: Su-Hwa
authors.initials: SH
authors.lastname: Chang
authors.forename: Liang-Yu
authors.initials: LY
authors.lastname: Chen
authors.forename: Wen-Yih
authors.initials: WY
authors.lastname: Chen
mesh_terms: D000388:Air; D000818:Animals; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry; D012996:Solutions; D013499:Surface Properties
chemical_list: D011506:Proteins; D012996:Solutions