Related ArticlesDNP NMR spectroscopy reveals new structures, residues and interactions in wild spider silks.
Chem Commun (Camb). 2019 Apr 16;55(32):4687-4690
Authors: Craig HC, Blamires SJ, Sani MA, Kasumovic MM, Rawal A, Hook JM
Abstract
DNP solid state NMR spectroscopy allows non-targeted analysis of wild spider silk in unprecedented detail at natural abundance, revealing hitherto unreported features across several species. A >50-fold signal enhancement for each silk, enables the detection of novel H-bonding networks and arginine conformations, and the post-translational modified amino acid, hydroxyproline.
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[ASAP] Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
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https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00552/20180703/images/medium/bi-2018-005525_0008.gif
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Authors: Sarker M, Orrell KE, Xu L, Tremblay ML, Bak JJ, Liu XQ, Rainey JK
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Aciniform silk protein (AcSp1) is the primary component of wrapping silk, the toughest of the spider silks due to combined high tensile strength and extensibility. Argiope trifasciata AcSp1 contains a core repetitive domain with...
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Solid-state nuclear magnetic resonance (NMR) has been extensively used to elucidate spider silk protein structure and dynamics. In many of these studies, site-specific isotope enrichment is critical for designing particular NMR methods...
DNP NMR spectroscopy reveals new structures, residues and interactions in wild spider silks.
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