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Adsorption Kinetics of Low Density Lipoprotein onto a Hydrophobic-Hydrophilic Gradient Surface

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Supramolecular Structure and Function 7

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Abstract

A subtle interplay between polar and non-polar interactions governs protein stability in aqueous solutions (Branden and Tooze, 1991). It also plays a decisive role in determining the interfacial property of proteins. For example, many small globular proteins such as a-lactalbumin, lysozyme and others, can not pack all their hydrophobic residues inside the protein core: these residues are often found exposed to the aqueous solution (Haynes and Norde, 1995). This exposure is energetically costly as the water molecules in the vicinity of protein hydrophobic residues lose some of their entropy relative to the bulk water. The free energy of the system will decrease when the exposed hydrophobic residue binds to another hydrophobic entity, or when it makes contact with a hydrophobic surface.

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Author information

Authors and Affiliations

  1. Department of Bioengineering, University of Utah, Salt Lake City, UT, 84112, USA

    Vladimir Hlady

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  1. Vladimir Hlady
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Editors and Affiliations

  1. Rudjer Bošković Institute, Zagreb, Croatia

    Greta Pifat-Mrzljak

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© 2001 Springer Science+Business Media New York

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Hlady, V. (2001). Adsorption Kinetics of Low Density Lipoprotein onto a Hydrophobic-Hydrophilic Gradient Surface. In: Pifat-Mrzljak, G. (eds) Supramolecular Structure and Function 7. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1363-6_4

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  • DOI: https://doi.org/10.1007/978-1-4615-1363-6_4

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5517-5

  • Online ISBN: 978-1-4615-1363-6

  • eBook Packages: Springer Book Archive

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