By Martin Malmsten
Totally up to date and improved chapters amassing fabric surrounding new and interesting concepts for harnessing and a biopolymer interfacial habit. beneficial properties learn contributions from approximately 60 profession's so much distinctive foreign specialists.
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Extra info for Biopolymers at interfaces / edited by Martin Malmsten
For larger proteins, which have a smaller surface/volume ratio the apolar fraction of the surface is usually less. Furthermore, water-soluble, nonaggregating proteins show a more or less even distribution of the polar and apolar residues over their surface so that no pronounced hydrophobic patches are present. Several studies [31,61,62] confirm that the hydrophobicity of the protein influences its adsorption. However, not only the hydrophobicity of the protein surface, but the overall hydrophobicity of the protein may be relevant for the adsorption behavior.
Hence, adsorption takes place only if the loss in conformational entropy is compensated by sufficient attraction between polymer segments and the surface. The critical Gibbs energy for adsorption to occur spontaneously is typically a few tenths of a kT unit per segment. Even if the Gibbs energy of adsorption is only slightly higher than the critical value, the whole polymer molecule adsorbs tenaciously and, apparently, irreversibly. This is because the contribution from each adsorbing segment adds to the Gibbs energy of adsorption of the whole polymer molecule.
Soc. 79:5333–5339 (1957). © 2003 by Marcel Dekker, Inc. Driving Forces for Protein Adsorption 6. 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 19. 20. 21. 22. 23. 24. 25. 26. 27. 28. 29. 41 C. Tanford and J. G.
Biopolymers at interfaces / edited by Martin Malmsten by Martin Malmsten