What does this research mean for the field?

The COOH-terminal half of rabbit skeletal tropomyosin features a repeating seven-residue pattern of nonpolar amino acids that enables its polypeptide chains to pack into a parallel coiled-coil structure, likely in a staggered arrangement to maximize hydrophobic interactions. Novelty: ClaimNovelty.CONFIRMATORY. Consensus alignment: ConsensusAlignment.NEUTRAL.

December 1, 1972Proceedings of the National Academy of SciencesOpen Access

Amino-Acid Sequence of Rabbit Skeletal Tropomyosin and Its Coiled-Coil Structure

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Authors

JSJaro Sodek RHRobert S. Hodges LSLawrence B. Smillie

Discussion

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Overview

Supports tropomyosin structural models in muscle; leaves open functional roles in cardiac regulation.

Key Points

Key points are not available for this paper at this time.

Cite This Study

Sodek et al. (1972) studied this question.

synapsesocial.com/papers/6a175df31723722a886e8f4c https://doi.org/10.1073/pnas.69.12.3800

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December 1, 1972Proceedings of the National Academy of SciencesOpen Access

Amino-Acid Sequence of Rabbit Skeletal Tropomyosin and Its Coiled-Coil Structure

View Full Paper

Ask AI

Bookmark

Authors

JSJaro Sodek RHRobert S. Hodges LSLawrence B. Smillie

Discussion

Member takes

Overview

Supports tropomyosin structural models in muscle; leaves open functional roles in cardiac regulation.

Key Points

Key points are not available for this paper at this time.

Cite This Study

Sodek et al. (1972) studied this question.

synapsesocial.com/papers/6a175df31723722a886e8f4c https://doi.org/10.1073/pnas.69.12.3800

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