Increasing IgG concentration modulates the conformational heterogeneity and bonding network that influence solution properties.
作者： Tim J. Kamerzell , Sonoko Kanai , Jun Liu , Steven J. Shire , Y. John Wang
DOI: 10.1021/JP9001548
关键词:
摘要: Multiple molecular driving forces mediate protein stability, association, and recognition in concentrated solutions. Here we investigate the interactions that modulate nonideal solution behavior of two immunoglobulins (IgG1s) highly solutions using two-dimensional vibrational correlation spectroscopy (2D-COS) principal components analysis (PCA). A specific sequence changes is observed concentration-dependent spectra viscous IgG deviates from ideality, whereas reversed for all other conditions examined. The asynchronous reveal variation β-sheet turn regions occur before intensity variations disordered α-helical as concentration increased regime. This contrast to studied idea are resistant affects. Finally, show hydrogen bonding an...
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