Kinetics of protein unfolding at interfaces

The conformation of protein molecules is determined by a balance of various forces, including van der Waals attraction, electrostatic interaction, hydrogen bonding, and conformational entropy.When protein molecules encounter an interface, they are often adsorbed on the interface.The conformation of an adsorbed protein molecule strongly depends on the interaction between the protein and the interface.Recent time-resolved investigations have revealed that protein conformation changes during the adsorption process due to the protein-protein interaction increasing with increasing interface coverage.External conditions also affect the protein conformation.This review considers recent dynamic observations of protein adsorption at various interfaces and their implications for the kinetics of protein unfolding at interfaces.Contents 1. Introduction 1 2. Experimental techniques 2 2.1.Adsorbed amount determination 2 2.2.Rate constant determination 3 2.3.Secondary structure determination 3 2.4.Molecular orientation determination 4 2.5.Tertiary structure determination 4 3. Brief description of theoretical approaches 4 4. Adsorption process 5 4.1.Classification of adsorption of proteins on hydrophobic interfaces 5 4.2.Protein adsorption at hydrophilic interfaces 9 5. Effects of external conditions 9 5.1.Protein concentration 9 5.2.Temperature 9 5.3.Electrostatics: pH and ionic strength 9 5.4.Additives 10 6.Conclusion