Signal peptide hydrophobicity is finely tailored for function
- 1 June 1994
- journal article
- research article
- Published by Wiley in Journal of Cellular Biochemistry
- Vol. 55 (2) , 209-217
- https://doi.org/10.1002/jcb.240550208
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Titration of protein transport activity by incremental changes in signal peptide hydrophobicityBiochemistry, 1993
- Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coliJournal of Bacteriology, 1990
- Novel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptideJournal of Bacteriology, 1989
- IDENTIFYING NONPOLAR TRANSBILAYER HELICES IN AMINO ACID SEQUENCES OF MEMBRANE PROTEINSAnnual Review of Biophysics, 1986
- Exploring the conformational roles of signal sequences: synthesis and conformational analysis of .lambda. receptor protein wild-type and mutant signal peptidesBiochemistry, 1984
- Intragenic suppressor mutations that restore export of maltose binding protein with a truncated signal peptideCell, 1984
- Role for membrane potential in the secretion of protein into the periplasm of Escherichia coli.Proceedings of the National Academy of Sciences, 1981
- The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesisCell, 1981
- Conformational properties of L‐leucine, L‐isoleucine, and L‐norleucine side chains in L‐lysine copolymersBiopolymers, 1977
- Nuclear magnetic resonance investigation of the helix to random coil transformation in poly‐α‐amino acids. I. Poly‐L‐alanineBiopolymers, 1969