pH Induced Structural Modulation and Interfacial Activity of Hemoglobin at the Air/Water Interface
作者： Mrityunjoy Mahato , Prabir Pal , Tapanendu Kamilya , Ratan Sarkar , G. B. Talapatra
DOI: 10.1021/JP908081R
关键词: Isoelectric point 、 Kinetics 、 Diffusion 、 Adsorption 、 Inorganic chemistry 、 Protonation 、 Monolayer 、 Intermolecular force 、 Deprotonation 、 Chemistry 、 Chromatography
摘要: In this Article, we report the surface activity of human globular blood protein, hemoglobin (Hb), at air/water interface. The Langmuir−Blodgett technique is used for monolayer characterization. adsorption growth-kinetics study shows that process interface involved with two mechanisms: one diffusion and other rearrangement unfolding. kinetics found to be dependent on pH protein concentration in subphase. CD FTIR studies suggest larger intermolecular aggregate β-sheet formation film lifted from air/acidic water alkaline isoelectric (6.8), not much variation observed. FE-SEM images support observation. acidic induced such conformational changes, aggregation explained argument α-helix conversion as well competition between protonation deprotonation aromatic-amino acid residues
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