Publications

the function of a leader peptide in translocating charged amino acyl residues across a membrane.	insertion of bacteriophage coat proteins into the membrane of infected bacterial cells can be studied as a model system of protein translocation across membranes. the coat protein of the filamentous bacteriophage pf3--which infects pseudomonas aeruginosa--is 44 amino acids in length and has the same basic structure as the coat protein of bacteriophage m13, which infects escherichia coli. however, unlike the pf3 coat protein, the m13 coat protein is synthesized as a precursor (procoat) with a typ ...	1990	2124001
characterization of the pf3 single-strand dna binding protein by circular dichroism spectroscopy.	we have used circular dichroism (cd) spectroscopy and gel electrophoresis to characterize the single-strand dna binding protein (ssdbp) of the bacteriophage pf3 and its complexes with pf3 dna and various dna and rna homopolymers. the secondary structure of pf3 ssdbp had < 1% alpha-helix and therefore was probably a beta-sheet structure like the fd gene 5 protein (g5p). from cd titrations, the binding stoichiometry of pf3 ssdbp was two nucleotides per protein monomer (n = 2) for complexes formed ...	1993	8241145
negatively charged amino acid residues play an active role in orienting the sec-independent pf3 coat protein in the escherichia coli inner membrane.	the coat protein of pseudomonas aeruginosa phage pf3 is transiently inserted into the bacterial inner membrane with a single transmembrane anchor sequence in the n(out)c(in) orientation. the n-terminal sequence immediately flanking the membrane anchor contains one negatively charged residue, whereas the c-terminal hydrophilic segment has two positively charged residues. to investigate how the orientation of this protein is achieved, the three flanking charged amino acid residues were altered. me ...	1997	9171335