Structural Proteins from Whelk Egg Capsule with Long Range Elasticity Associated with a Solid-State Phase Transition

S. Scott Wasko; Gavin Tay; Andreas Schwaighofer; Christoph Nowak; J. Herbert Waite; Ali Miserez

doi:10.1021/bm401598z

Structural Proteins from Whelk Egg Capsule with Long Range Elasticity Associated with a Solid-State Phase Transition

S. Scott Wasko, Gavin Tay, Andreas Schwaighofer, Christoph Nowak, J. Herbert Waite, Ali Miserez

Research output: Contribution to journal › Article › peer-review

Abstract

The robust, proteinaceous egg capsules of marine prosobranch gastropods (genus Busycotypus) exhibit unique biomechanical properties such as high elastic strain recovery and elastic energy dissipation capability. Capsule material possesses long-range extensibility that is fully recoverable and is the result of a secondary structure phase transition from α-helical coiled-coil to extended β-sheet rather than of entropic (rubber) elasticity. We report here the characterization of the precursor proteins that make up this material. Three different proteins have been purified and analyzed, and complete protein sequences deduced from messenger ribonucleic acid (mRNA) transcripts. Circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy indicate that the proteins are strongly α-helical in solution and primary sequence analysis suggests that these proteins have a propensity to form coiled-coils. This is in agreement with previous wide-angle X-ray scattering (WAXS) and solid-state Raman spectroscopic analysis of mature egg capsules.

Original language	English
Number of pages	13
Journal	Biomacromolecules
DOIs	https://doi.org/10.1021/bm401598z
Publication status	Published - 2014

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Biosensor Technologies

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title = "Structural Proteins from Whelk Egg Capsule with Long Range Elasticity Associated with a Solid-State Phase Transition",

abstract = "The robust, proteinaceous egg capsules of marine prosobranch gastropods (genus Busycotypus) exhibit unique biomechanical properties such as high elastic strain recovery and elastic energy dissipation capability. Capsule material possesses long-range extensibility that is fully recoverable and is the result of a secondary structure phase transition from α-helical coiled-coil to extended β-sheet rather than of entropic (rubber) elasticity. We report here the characterization of the precursor proteins that make up this material. Three different proteins have been purified and analyzed, and complete protein sequences deduced from messenger ribonucleic acid (mRNA) transcripts. Circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy indicate that the proteins are strongly α-helical in solution and primary sequence analysis suggests that these proteins have a propensity to form coiled-coils. This is in agreement with previous wide-angle X-ray scattering (WAXS) and solid-state Raman spectroscopic analysis of mature egg capsules.",

author = "Wasko, {S. Scott} and Gavin Tay and Andreas Schwaighofer and Christoph Nowak and Waite, {J. Herbert} and Ali Miserez",

year = "2014",

doi = "10.1021/bm401598z",

language = "English",

journal = "Biomacromolecules",

issn = "1525-7797",

publisher = "American Chemical Society",

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T1 - Structural Proteins from Whelk Egg Capsule with Long Range Elasticity Associated with a Solid-State Phase Transition

AU - Wasko, S. Scott

AU - Tay, Gavin

AU - Schwaighofer, Andreas

AU - Nowak, Christoph

AU - Waite, J. Herbert

AU - Miserez, Ali

PY - 2014

Y1 - 2014

N2 - The robust, proteinaceous egg capsules of marine prosobranch gastropods (genus Busycotypus) exhibit unique biomechanical properties such as high elastic strain recovery and elastic energy dissipation capability. Capsule material possesses long-range extensibility that is fully recoverable and is the result of a secondary structure phase transition from α-helical coiled-coil to extended β-sheet rather than of entropic (rubber) elasticity. We report here the characterization of the precursor proteins that make up this material. Three different proteins have been purified and analyzed, and complete protein sequences deduced from messenger ribonucleic acid (mRNA) transcripts. Circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy indicate that the proteins are strongly α-helical in solution and primary sequence analysis suggests that these proteins have a propensity to form coiled-coils. This is in agreement with previous wide-angle X-ray scattering (WAXS) and solid-state Raman spectroscopic analysis of mature egg capsules.

AB - The robust, proteinaceous egg capsules of marine prosobranch gastropods (genus Busycotypus) exhibit unique biomechanical properties such as high elastic strain recovery and elastic energy dissipation capability. Capsule material possesses long-range extensibility that is fully recoverable and is the result of a secondary structure phase transition from α-helical coiled-coil to extended β-sheet rather than of entropic (rubber) elasticity. We report here the characterization of the precursor proteins that make up this material. Three different proteins have been purified and analyzed, and complete protein sequences deduced from messenger ribonucleic acid (mRNA) transcripts. Circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy indicate that the proteins are strongly α-helical in solution and primary sequence analysis suggests that these proteins have a propensity to form coiled-coils. This is in agreement with previous wide-angle X-ray scattering (WAXS) and solid-state Raman spectroscopic analysis of mature egg capsules.

U2 - 10.1021/bm401598z

DO - 10.1021/bm401598z

M3 - Article

SN - 1525-7797

JO - Biomacromolecules

JF - Biomacromolecules

ER -

Structural Proteins from Whelk Egg Capsule with Long Range Elasticity Associated with a Solid-State Phase Transition

Abstract

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