Polymeric sequences reveal a functional interrelationship between hydrophobicity and length of signal peptides.

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Article

Polymeric sequences reveal a functional interrelationship between hydrophobicity and length of signal peptides.

The Journal of biological chemistry - 15 Feb 1990

Chou M M, Kendall D A

Abstract excerpt

We have examined the hydrophobicity component of signal peptide function using polymeric sequences in combination with cassette mutagenesis. Using homopolymeric units of either isoleucine, leucine, valine or alanine to replace the natural core segment of the Escherichia coli alkaline phosphatase...

Topics

Alkaline Phosphatase
Amino Acid Sequence
Base Sequence
DNA Transposable Elements
Escherichia coli
Kinetics
Molecular Sequence Data
Mutation
Oligonucleotide Probes
Plasmids
Protein Conformation
Protein Processing, Post-Translational
Protein Sorting Signals
Recombinant Proteins

Source

Open in PubMed

Identifiers

PMID: 2154463

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2154463-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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