title: Internal stark effect measurement of the electric field at the amino terminus of an alpha helix.
abstract: The strengths of electrostatic interactions in biological molecules are difficult to calculate or predict because they occur in complicated, inhomogeneous environments. The electric field at the amino terminus of an alpha helix in water has been determined by measuring the shift in the absorption band for a covalently attached, neutral probe molecule with an electric dipole moment difference between the ground and excited electronic states (an internal Stark effect). The field at the interface between the helix and the solvent is found to be an order of magnitude stronger than expected from the dielectric properties of bulk water. Furthermore, although the total electric dipole moment of the helix increases with length, the electric field at the amino terminus does not.
authors.affiliation: Department of Biology, Massachusetts Institute of Technology, Nine Cambridge Center 02142.
authors.forename: D J
authors.initials: DJ
authors.lastname: Lockhart
authors.forename: P S
authors.initials: PS
authors.lastname: Kim
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D004563:Electrochemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D014867:Water
chemical_list: D000596:Amino Acids; D010455:Peptides; D011506:Proteins; D014867:Water