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The designed 29-residue peptide coil-VaLd forms a parallel three-helix bundle driven by a hydrophobic core of alternating valine and leucine layers, which stack head-to-tail to form a continuous coiled coil that can serve as a basis for engineering peptide crystals. Novelty: ClaimNovelty.NOVEL_FINDING. Consensus alignment: ConsensusAlignment.NEUTRAL.

January 1, 1997Protein ScienceOpen Access

The crystal structure of the designed trimeric coiled coil coil‐VaLd: Implications for engineering crystals and supramolecular assemblies

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Authors

NON.L. OgiharaUC Davis Comprehensive Cancer Center MWM.S. WeissHelmholtz-Zentrum Berlin für Materialien und Energie

David EisenbergRutgers, The State University of New Jersey

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Ogihara et al. (1997) studied this question.

synapsesocial.com/papers/6a0a50ceac8a0d6c3ab4e84f https://doi.org/10.1002/pro.5560060109

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The crystal structure of the designed trimeric coiled coil coil‐VaLd: Implications for engineering crystals and supramolecular assemblies

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Cite This Study

The crystal structure of the designed trimeric coiled coil coil‐VaLd: Implications for engineering crystals and supramolecular assemblies

Discussion

Member takes

Implication

Key Points

Cite This Study

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