Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10230096 | Biomaterials | 2005 | 6 Pages |
Abstract
To obtain a better understanding of factors controlling cross-linking rates of Mussel adhesive proteins, we study the conformation of the Mussel Adhesive Protein Mefp-1. The dimensions of Mefp-1 in solution are determined by dynamic light scattering. Under physiological conditions, the hydrodynamic radius RH of Mefp-1 is found to be 10.5±1.1 nm. Measured Mefp-1 dimensions are compared with theoretical dimensions of Mefp-1 in random coil conformations. We have strong indications that Mefp-1, under dilute and physiological conditions, has a self-avoiding random walk conformation with helix-like deca-peptide segments. With a number of segments of approximately 90, the segment length is found to be 2.7 nm.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Sander Haemers, Mieke C. van der Leeden, Gert Frens,