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Fluorescence Study Of A Mutant Cytochrome-b5 With A Single Tryptophan In The Membrane-binding Domain

Fluorescence studies of cytochrome b5 are complicated by the presence of three tryptophans, at positions 108, 109, and 112, in the membrane-binding domain. The cDNA for rabbit liver cytochrome b5, isolated from a lambda-gt11 library, was used to…

Tags: 1991, b5, BIOCHEMISTRY, Biochemistry & Molecular Biology, energy, Holloway P W, indole, Journal Article or Conference Abstract Publication, Ladokhin A S, Mutagenesis, probes, residue, Spectroscopy, Steggles A W, vesicles, Wang L

Biophysical Studies Of Cytochromes-b5 With Amino-acid Substitutions In The Membrane-binding Domain

Tags: 1992, Biophysical Journal, Biophysics, Holloway P W, Journal Article or Conference Abstract Publication, Ladokhin A S, probes, Steggles A W, topography, transform infrared-spectroscopy, Tretyachenkoladokhina V G, Wang L

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