title: Structural information of mussel adhesive protein Mefp-3 acquired at various polymer/Mefp-3 solution interfaces.
abstract: Mytilus edulis foot protein Mefp-3 serves as a primer in the formation of adhesive plaques that attach the mussel to solid surfaces in its immediate environment. The adsorption behavior of this protein on various materials of different hydrophobicity was studied using sum frequency generation (SFG) vibrational spectroscopy. By collecting SFG signals from side chains of these amino acids and from secondary structures of the protein, we have determined that this protein adopts different conformations at different interfaces, depending on hydrophobicity of the contact medium and specific chemical group interactions. We have also demonstrated that SFG has the potential to track the interfacial conformations of a single amino acid in a protein.
authors.affiliation: Department of Chemistry, 930 North University Avenue, University of Michigan, Ann Arbor, MI 48109, USA.
authors.forename: Mark A
authors.initials: MA
authors.lastname: Even
authors.forename: Jie
authors.initials: J
authors.lastname: Wang
authors.forename: Zhan
authors.initials: Z
authors.lastname: Chen
mesh_terms: D000327:Adsorption; D000818:Animals; D002942:Circular Dichroism; D057927:Hydrophobic and Hydrophilic Interactions; D049880:Mytilus edulis / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011108:Polymers; D011506:Proteins