Article
Idealization of the hydrophobic segment of the alkaline phosphatase signal peptide.
Nature - 1 Jan 2000
Kendall D A, Bock S C, Kaiser E T
Abstract excerpt
Proteins secreted by prokaryotic cells are synthesized as precursors containing an amino-terminal extension sequence or signal peptide. Although these signal peptides share little primary sequence homology, recent studies suggest that they function via common pathways during the transport process and that a common element may reside in their secondary structural characteristics. We are investigating the role of...
Topics
- Alkaline Phosphatase
- Amino Acid Sequence
- Escherichia coli
- Mutation
- Protein Conformation
- Protein Processing, Post-Translational
- Protein Sorting Signals
- Solubility
- Structure-Activity Relationship