Coil dimensions of the mussel adhesive protein Mefp-1.
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.
Department of Radiochemistry, Interfaculty Reactor Institute, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands.
Sander
S
Haemers
Mieke C
MC
van der Leeden
Gert
G
Frens
D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry; D049872:Bivalvia / Q000378:metabolism*; D002942:Circular Dichroism; D003198:Computer Simulation; D008422:Materials Testing; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000032:analysis* / Q000737:chemistry*
D001672:Biocompatible Materials; D011506:Proteins; C037403:adhesive protein, mussel