The adsorption of human carbonic anhydrase II pseudo-wild type (HCAIIpwt) and an N-terminally truncated version thereof onto silica surfaces were studied. The amount adsorbed and the adsorption kinetics were measured using in situ ellipsometry. A substantial difference was seen between the two proteins. The adsorbed amount of the truncated version (2.53 mg/m2) indicates an end-on orientation, while the HCAIIpwt seems to adsorb side-on (1.84 mg/m2). It is suggested that the orientation effects arise from the truncation. The truncation is known to unfold the two most N-terminal helical segments, which could inhibit adsorption with the N-terminal region facing the surface, due to steric repulsion.
|Title of host publication||The Colloid Science of Lipids New Paradigms for Self-Assembly in Science and Technology|
|Editors||B. Lindman, B. W. Ninham|
|Number of pages||5|
|Publication status||Published - 1998|
|Name||Progress in Colloid & Polymer Science book series, PROGCOLLOID|