Intramembrane position of the fluorescent tryptophanyl residue in membrane-bound cytochrome b5
- 1 November 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (24) , 5458-5464
- https://doi.org/10.1021/bi00591a031
Abstract
A method was developed to measure the intramembrane position of the fluorescent tryptophanyl residue in whole [steer liver] cytochrome b5 and the nonpolar membrane binding segment when these molecules are bound to phospholipid vesicles. The method utilizes excitation energy transfer from the donor tryptophanyl residue in the protein to trinitrophenyl or dansyl acceptor groups on the surface of the phospholipid bilayer. The single fluorescent tryptophanyl residue in vesicle-bound cytochrome b5 and the nonpolar segment is located approximately 20-22 .ANG. below the surface of the bilayer. This position represents a minimum depth of penetration of this portion of the cytochrome in the membrane.This publication has 5 references indexed in Scilit:
- The binding of cytochrome b5 to phospholipid vesicles and biological membranes. Effect of orientation on intermembrane transfer and digestion by carboxypeptidase Y.Journal of Biological Chemistry, 1979
- The orientational freedom of molecular probes. The orientation factor in intramolecular energy transferBiophysical Journal, 1979
- Structural and functional properties of the membrane binding segment of cytochrome b5.Journal of Biological Chemistry, 1978
- The primary structure of the nonpolar segment of bovine cytochrome b5Journal of Biological Chemistry, 1978
- Physical properties of the dimyristoylphosphatidylcholine vesicle and of complexes formed by its interaction with apolipoprotein C-IIIBiochemistry, 1977