The Amino-terminal Charge and Core Region Hydrophobicity Interdependently Contribute to the Function of Signal Sequences
Open Access
- 1 August 1996
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (35) , 21579-21582
- https://doi.org/10.1074/jbc.271.35.21579
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Physical and Conformational Properties of Synthetic Idealized Signal Sequences Parallel Their Biological FunctionBiochemistry, 1995
- SecA-dependence of the translocation of a large periplasmic loop in theEscherichia coliMalF inner membrane protein is a function of sequence contextMolecular Membrane Biology, 1995
- Signal peptide hydrophobicity is finely tailored for functionJournal of Cellular Biochemistry, 1994
- Titration of protein transport activity by incremental changes in signal peptide hydrophobicityBiochemistry, 1993
- Signal sequencesBiochemistry, 1989
- Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranesNature, 1988
- Net N-C charge imbalance may be important for signal sequence function in bacteriaJournal of Molecular Biology, 1986
- Idealization of the hydrophobic segment of the alkaline phosphatase signal peptideNature, 1986
- Predicted secondary structures of amino‐terminal extension sequences of secreted proteinsFEBS Letters, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970