The contributions of the time-dependent changes in oil molecules conformations on time-dependent conformational changes of proteins at oil-'protein solution' interface was studied using ATR (Attenuated Total Reflection)-FTIR spectroscopic technique. Conformational changes of Bacillus Subtilis extracellular proteins (BSEPs), Fibronectin and Bovine serum albumin (BSA) at hexane-'protein solution' system was compared. The IR spectra collected on the protein aggregate - film - formed at the hexane-'protein solution' interface demonstrated time-dependent conformational changes of the proteins through changes in the shapes and positions of the H2O-'amide I' cross peaks and the amide II peaks as a function of time (0-90th minute). Hexane-protein intermolecular association in the film was evident as the CH stretching vibration peaks of hexane were present along with the amide peaks in all the spectra collected over a period of 90 minutes. Conformational changes of the hexane molecules, along with that of the proteins, were observed via variations (broadening and red/blue shifts) in the CH stretching vibration peaks of the CH3 and the CH2 groups of hexane. The red/blue shifts of the CH stretching vibration peaks of hexane were different with BSEPs, Fibronectin and BSA, further indicating that the conformational changes of hexane molecules being protein specific. As similar to the protein types considered here, at oil-'protein solution' interfaces, conformational changes of the oil molecules appears to be a regular phenomenon and possibly play a key role in regulating the protein conformational changes at Oil-Water interface. This result provide new insights onto the understanding of the role of phospholipids conformations on cell membrane protein dynamics.

Role of the conformational changes of the oil molecules on the protein conformational changes at oil-water interfaces

248th National Meeting (2014)

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