By Martin Malmsten
Totally up to date and elevated chapters accumulating fabric surrounding new and interesting concepts for harnessing and a biopolymer interfacial habit. positive aspects learn contributions from approximately 60 profession's such a lot exclusive foreign experts.
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Additional resources for Biopolymers at interfaces / edited by Martin Malmsten
14:1–63 (1959). E. M. Richards, Areas, volumes, packing and protein structure. Ann. Rev. Biophysics. Bioeng. 6:151–176 (1977). B. Lee and F. M. Richards, The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:379–400 (1971). C. Tanford and J. G. Kirkwood, Theory of protein titration curves. I. General equations for impenetrable spheres. J. Am. Chem. Soc. 79:5333–5339 (1957). © 2003 by Marcel Dekker, Inc. Driving Forces for Protein Adsorption 6. 7. 8. 9. 10.
Ellipsometry and reflectometry, determine an optical thickness (Ϸ average loop extension), whereas other methods, such as dynamic light scattering and viscometry, yield the hydrodynamic thickness (Ϸ tail extension). Invariably, the tails extend further from the sorbent surface than the average of the loops. Based on these considerations the adsorption behavior of flexible polyelectrolytes may be predicted. Because of the charge they carry, polyelectrolytes are strongly expanded in aqueous solution; in other words water is an excellent solvent for flexible polyelectrolytes.
The experimental thickness of the adsorbed polymer layer depends on the method of determination. , ellipsometry and reflectometry, determine an optical thickness (Ϸ average loop extension), whereas other methods, such as dynamic light scattering and viscometry, yield the hydrodynamic thickness (Ϸ tail extension). Invariably, the tails extend further from the sorbent surface than the average of the loops. Based on these considerations the adsorption behavior of flexible polyelectrolytes may be predicted.
Biopolymers at interfaces / edited by Martin Malmsten by Martin Malmsten