By Martin Malmsten
Totally up to date and improved chapters amassing fabric surrounding new and fascinating concepts for harnessing and a biopolymer interfacial habit. good points learn contributions from approximately 60 profession's so much exceptional overseas experts.
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Additional resources for Biopolymers at interfaces / edited by Martin Malmsten
Finally, it should be realized that all these approaches, except the one by Noinville et al. , are based on continuum models. , the sorbent surface, the protein molecule, and the solvent, are treated as continuous media having their own, constant dielectric permittivity, and in each of the phases the charge is smeared out according to the assumed distribution. However, in reality, in particular at high ionic strength, the distances between the individual charged groups on the protein and on the sorbent surface may exceed the Debye length, so a discrete-charge model would be more appropriate.
Furthermore, the electrolyte concentration largely affects the distance over which charged groups interact. © 2003 by Marcel Dekker, Inc. Driving Forces for Protein Adsorption 27 FIG. 5 Ordering of polypeptide chains into an ␣-helix structure (left) and a parallel ␤-pleated sheet (right). If charged residues are present in the interior of a globular protein molecule, they usually occur as ion pairs. Unfolding of the protein would imply rupture of the electrostatically favorable ion pairs but also leads to favorable hydration of both ionic groups.
2 Driving Forces for Protein Adsorption at Solid Surfaces WILLEM NORDE The Netherlands I. Wageningen Agricultural University, Wageningen, INTRODUCTION Proteins are copolymers of some 22 different amino acids of varying hydrophobicity (Fig. 1). As a consequence, proteins are more or less amphiphilic and, therefore, usually highly surface active. Moreover, a number of amino acid residues in the side groups along the polypeptide chain contain positive or negative charges. This makes the protein an amphoteric polyelectrolyte.
Biopolymers at interfaces / edited by Martin Malmsten by Martin Malmsten