Elucidating metabolic pathways for amino acid incorporation into dragline spider silk using 13C enrichment and solid state NMR
نویسندگان
چکیده
منابع مشابه
Elucidating proline dynamics in spider dragline silk fibre using 2H-13C HETCOR MAS NMR.
(2)H-(13)C HETCOR MAS NMR is performed on (2)H/(13)C/(15)N-Pro enriched A. aurantia dragline silk. Proline dynamics are extracted from (2)H NMR line shapes and T1 in a site-specific manner to elucidate the backbone and side chain molecular dynamics for the MaSp2 GPGXX β-turn regions for spider dragline silk in the dry and wet, supercontracted states.
متن کاملAnalysis of repetitive amino acid motifs reveals the essential features of spider dragline silk proteins
The extraordinary mechanical properties of spider dragline silk are dependent on the highly repetitive sequences of the component proteins, major ampullate spidroin 1 and 2 (MaSp2 and MaSp2). MaSp sequences are dominated by repetitive modules composed of short amino acid motifs; however, the patterns of motif conservation through evolution and their relevance to silk characteristics are not wel...
متن کاملNanostructure and molecular mechanics of spider dragline silk protein assemblies.
Spider silk is a self-assembling biopolymer that outperforms most known materials in terms of its mechanical performance, despite its underlying weak chemical bonding based on H-bonds. While experimental studies have shown that the molecular structure of silk proteins has a direct influence on the stiffness, toughness and failure strength of silk, no molecular-level analysis of the nanostructur...
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Rising, A. 2007. Spider dragline silk – molecular properties and recombinant production. Doctor’s dissertation. ISSN: 1652-6880, ISBN: 978-91-576-7337-4 Spider dragline silk possesses several desirable features of a biomaterial; it has extraordinary mechanical properties, is biocompatible and biodegradable. It consists of large proteins, major ampullate spidroins (MaSp:s), that contain alternat...
متن کاملSupramolecular interactions probed by 13C-13C solid-state NMR spectroscopy.
We present a robust solid-state NMR approach for the accurate determination of molecular interfaces in insoluble and noncrystalline protein-protein complexes. The method relies on the measurement of intermolecular (13)C-(13)C distances in mixtures of [1-(13)C]glucose- and [2-(13)C]glucose-labeled proteins. We have applied this method to Parkinson's disease-associated α-synuclein fibrils and fou...
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ژورنال
عنوان ژورنال: Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology
سال: 2011
ISSN: 1095-6433
DOI: 10.1016/j.cbpa.2011.02.010