page_title: Protein adsorption
section_title: Conformation effects
hierarchical_section_title: Protein adsorption / Protein adsorption to polymers / Conformation effects
caption_attribution_description: English: Illustration of how protein conformational changes as a result of adsorption can change ligand binding sites.
context_page_description: Adsorption is the accumulation and adhesion of molecules, atoms, ions, or larger particles to a surface, but without surface penetration occurring. The adsorption of larger biomolecules such as proteins is of high physiological relevance, and as such they adsorb with different mechanisms than their molecular or atomic analogs. Some of the major driving forces behind protein adsorption include: surface energy, intermolecular forces, hydrophobicity, and ionic or electrostatic interaction. By knowing how these factors affect protein adsorption, they can then be manipulated by machining, alloying, and other engineering techniques to select for the most optimal performance in biomedical or physiological applications.
context_section_description: Protein adsorption often results in significant conformational changes, which refers to changes in the secondary, tertiary, and quartary structures of proteins.  In addition to adsorption rates and amounts, orientation and conformation are of critical importance.  These conformational changes can affect protein interaction with ligands, substrates, and antigens which are dependent on the orientation of the binding site of interest.  These conformational changes, as a result of protein adsorption, can also denature the protein and change its native properties.
caption: Illustration of protein (green) ligand (red star) binding site alteration by the conformational change of the protein as a result of surface (blue) adsorption. Note how the ligand no longer fits into the binding site.
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