Hydrophobic collapse

Protein Adhesives

Published in A. Pizzi, K. L. Mittal, Handbook of Adhesive Technology, 2017

Most proteins, including those used in adhesives, are globular proteins that have enough hydrophobic portions or weakly hydrophilic portions to cause the protein to fold inward in an aqueous environment (Figure 5.3). During this hydrophobic collapse, intramolecular association of hydrophobic amino acids moves them mainly to the inside of the globular structure and the polar amino acids preferentially to the outside. However, the primary and secondary structures limit the ability of particular amino acids to move to these separate regions. The polar groups on the inside of the globule are stabilized by associating with other polar groups on the chain. These types of interactions include not only hydrogen bonds, but also acid–base salt bridges and disulfides from the thiol groups. Some of the hydrophobic amino acids end up on the outside of the structure. This folding of the protein is referred to as its tertiary structure.

Exploration of ligand-induced protein conformational alteration, aggregate formation, and its inhibition: A biophysical insight

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Journal Information

Published in Preparative Biochemistry and Biotechnology, 2018

Saima Nusrat, Rizwan Hasan Khan

It is the most accepted model for the protein folding kinetics of globular proteins like myoglobin, alpha-lactalbumin, etc. Hydrophobic amino acid residues repel water molecules and forms hydrophobic bond between them, finally forming a hydrophobic collapse-like structure.[62]

Hydrophobic collapse

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Protein Adhesives

Exploration of ligand-induced protein conformational alteration, aggregate formation, and its inhibition: A biophysical insight