19F nuclear magnetic resonance studies of the coat protein of bacteriophage M13 in synthetic phospholipid vesicles and deoxycholate micelles.
The nonlytic, filamentous coliphage M13 offers an excellent model system for the study of membrane-protein interactions. We prepare derivatives of the protein containing fluorine-labeled amino acids and use 19F nuclear magnetic resonance (NMR) to study the protein in both deoxycholate micelles and phospholipid vesicles. We have previously described the in vivo preparation of an m-fluorotyrosyl derivative of M13 coat protein and also a method for incorporation of high levels of this protein into small, uniformly sized phospholipid vesicles of defined composition. Herein we describe the in vivo preparation and the characterization of an m-fluorophenylalanine derivative. We simultaneously compare the environment and mobility of the tyrosine and phenylalanine residues (the former in the hydrophobic region of the protein and the latter in the hydrophilic regions) as influenced by bile salt detergent or lipid interactions.
D003090:Coliphages / Q000648:ultrastructure*; D005461:Fluorine; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D008567:Membranes, Artificial; D008823:Micelles; D010649:Phenylalanine / Q000031:analogs & derivatives; D010743:Phospholipids; D014443:Tyrosine / Q000031:analogs & derivatives; D014764:Viral Proteins / Q000502:physiology*
D008567:Membranes, Artificial; D008823:Micelles; D010743:Phospholipids; D014764:Viral Proteins; C001245:3-fluorotyrosine; D005461:Fluorine; D014443:Tyrosine; C027218:3-fluorophenylalanine; D010649:Phenylalanine