Adsorption of human carbonic anhydrase II onto silicon oxides surfaces : The effects of truncation in the N-terminal region
(1998) In Progress in Colloid & Polymer Science book series, PROGCOLLOID 108. p.161-165- Abstract
- 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.
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- author
- Billsten, P ; Wahlgren, M LU and Elwing, H
- organization
- publishing date
- 1998
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- subject
- keywords
- Protein adsorption, Ellipsometry, Carbonic Anhydrases, Mutant proteins, Solid Surfaces
- host publication
- The Colloid Science of Lipids New Paradigms for Self-Assembly in Science and Technology
- series title
- Progress in Colloid & Polymer Science book series, PROGCOLLOID
- editor
- Lindman, B. and Ninham, B. W.
- volume
- 108
- pages
- 5 pages
- publisher
- Springer
- external identifiers
-
- scopus:0542369594
- ISSN
- 1435-1536
- 0340-255X
- ISBN
- 978-3-7985-1655-7
- 978-3-7985-1112-5
- DOI
- 10.1007/BFb0117973
- language
- English
- LU publication?
- yes
- id
- 5e5b67bd-60b9-42a5-89e8-69d258e164cf
- date added to LUP
- 2016-04-15 19:29:39
- date last changed
- 2024-01-03 23:50:30
@inproceedings{5e5b67bd-60b9-42a5-89e8-69d258e164cf, abstract = {{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.}}, author = {{Billsten, P and Wahlgren, M and Elwing, H}}, booktitle = {{The Colloid Science of Lipids New Paradigms for Self-Assembly in Science and Technology}}, editor = {{Lindman, B. and Ninham, B. W.}}, isbn = {{978-3-7985-1655-7}}, issn = {{1435-1536}}, keywords = {{Protein adsorption; Ellipsometry; Carbonic Anhydrases; Mutant proteins; Solid Surfaces}}, language = {{eng}}, pages = {{161--165}}, publisher = {{Springer}}, series = {{Progress in Colloid & Polymer Science book series, PROGCOLLOID}}, title = {{Adsorption of human carbonic anhydrase II onto silicon oxides surfaces : The effects of truncation in the N-terminal region}}, url = {{http://dx.doi.org/10.1007/BFb0117973}}, doi = {{10.1007/BFb0117973}}, volume = {{108}}, year = {{1998}}, }