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.
Haemers
Sander
S
Department of Radiochemistry, Interfaculty Reactor Institute, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands.
van der Leeden
Mieke C
MC
Frens
Gert
G
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