Hydrophobic interfaces unfolding

Fig. 7. Schematic illustration of free energy assignments for three different types of interactions. The examples illustrate the situation existing for folded, unfolded, and one partially folded intermediate. For hydrophobic interfaces, partially folded intermediates always include an extra term Ag corresponding to the solvent exposure of protein regions that have not undergone unfolding. The unfolded state lacks this uncompensated exposure term. For a bonded or liganded interface, cooperative behavior is created when the unfolding of either domain results in the disruption of the bonded interface or the dissociation of the ligand molecule. [Reprinted from Freire el al. (1991)].

Proteins often have the same high-affinity isotherms as do synthetic polymers and are also slow to equilibrate, due to many contacts with the surface. Proteins, however, have the additional complication that they can partially or completely unfold at the solid-liquid interface to expose their hydrophobic core units to a hydrophobic surface... 

Mechanical forces, such as shearing, shaking, and pressure, may also denature proteins [44,45], Shaking proteins may lead to inactivation owing to an increase in the area of the gas/liquid interface. At the interface, the protein unfolds and maximizes exposure of hydrophobic residues to the air. Surface denaturation may also occur at the protein/container interface and has been observed following adsorption of proteins to filter materials [46]. 

III) Once the protein is located at the interface, there is reorganization and exposure of the accessible hydrophobic sites on the protein to the hydrophobic phase, followed by changes in the conformation of the protein at the interface. As this takes place, slow macro-molecular reorganization via unfolding plays an important role, especially for globular proteins. 

Analysis of the crystallographic structure also reveals that the two domains interact primarily through hydrophobic and hydrogen bond interactions at the interface. The number of apolar hydrogens that become exposed on the C domain on unfolding of the N domain is 49.4, and the number of apolar hydrogens exposed on the N domain on unfolding of the C domain is 44.8. These values correspond to 726 and 659 A2 of apolar surface area, respectively. In addition, nine... 

Proteins are dynamic molecules with respect to structure. The preferred folded structure for a given set of environmental conditions is that which has the minimum free energy. The driving force to assume a given folded structure is a thermodynamic force. In aqueous systems, the hydrophobic side-chains will endeavour to orient away from the surrounding water and towards the core of the molecule. However, for high surface activity, it is essential that the protein molecule should unfold and orient its hydrophobic side-chains towards the oil phase. A lack of hydrophilic residues usually does not restrict protein functionality at interfaces. Thus, flexible proteins can create a highly hydrated, mobile layer to stabilize an emulsion particle. 

The loss of solubility of a protein at an interface and the observed area per residue suggested that the molecule unfolded and adopted the P conformation. This structure with intermolecular hydrogen bonds adequately accounted for the area observed and is still postulated by some workers (3). Cheesman and Davies (4) suggested other extended conformations with the orientation of the side chains largely determined by their hydrophobic or polar character. Their proposals, mainly based on early work on synthetic polypeptides, do not conform to present stereochemical criteria nor do they take account of the possibility that the a-helix or related helical conformations might be present. 

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