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Article

Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis.

Protein science : a publication of the Protein Society - 1 Jul 1993

Hu J C, Newell N E, Tidor B, Sauer R T

Abstract excerpt

Combinatorial mutagenesis with an alphabet limited to alanine, glutamic acid, lysine, and threonine was used to probe the role of interactions involving surface residues in stabilizing a short alpha-helical coiled coil. The residues at eight e and g positions in the leucine zipper of the Saccharomyces cerevisiae transcription factor GCN4 were randomized to these four residues in a lambda repressor-leucine zipper...

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Identifiers

PMID: 8102921
DOI: 10.1002/pro.5560020701
PMCID: PMC2142419

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis.PMID 8102921Read ↗

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