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Article

The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil.

Journal of molecular biology - 28 Jul 2000

Zhu H, Celinski S A, Scholtz J M, Hu J C

Abstract excerpt

The dimeric interface of the leucine zipper coiled coil from GCN4 has been used to probe the contributions of hydrophobic and hydrogen bonding interactions to protein stability. We have determined the energetics of placing Ile or Asn residues at four buried positions in a two-stranded coiled coil. As expected, Ile is favored over Asn at these buried positions, but not as much as predicted by considering only the...

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Source

Identifiers

PMID: 10903875
DOI: 10.1006/jmbi.2000.3936

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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