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Article

Prediction of quaternary structure of coiled coils. Application to mutants of the GCN4 leucine zipper.

Journal of molecular biology - 18 Aug 1995

Vieth M, Kolinski A, Brooks C L, Skolnick J

Abstract excerpt

Using a simplified protein model, the equilibrium between different oligomeric species of the wild-type GCN4 leucine zipper and seven of its mutants have been predicted. Over the entire experimental concentration range, agreement with experiment is found in five cases, while in two cases agreement is found over a portion of the concentration range. These studies demonstrate a methodology for predicting coiled...

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Identifiers

PMID: 7650742
DOI: 10.1006/jmbi.1995.0447

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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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Click a neighbor to travelStep 1 · 12 closest

Prediction of quaternary structure of coiled coils. Application to mutants of the GCN4 leucine zipper.PMID 7650742Read ↗

A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants.Semantic proximity Read ↗

An engineered leucine zipper a position mutant with an unusual three-state unfolding pathway.Semantic proximity Read ↗

An engineered allosteric switch in leucine-zipper oligomerization.Semantic proximity Read ↗

The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil.Semantic proximity Read ↗

Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat.Semantic proximity Read ↗

Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism.Semantic proximity Read ↗

Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions.Semantic proximity Read ↗

A hamiltonian replica exchange method for building protein-protein interfaces applied to a leucine zipper.Semantic proximity Read ↗

A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding.Semantic proximity Read ↗

Self-assembly of coiled-coil tetramers in the 1.40 A structure of a leucine-zipper mutant.Semantic proximity Read ↗

Buried polar residues and structural specificity in the GCN4 leucine zipper.Semantic proximity Read ↗

The magnitude of the backbone conformational entropy change in protein folding.Semantic proximity Read ↗

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