Related ArticlesPhosphate-silica interactions in diatom biosilica and synthetic composites studied by Rotational Echo Double Resonance (REDOR) NMR spectroscopy.
Langmuir. 2020 Apr 01;:
Authors: Kolbe F, Daus F, Geyer A, Brunner E
Abstract
Biosilica is a biogenic composite material produced by organisms like diatoms. Various biomolecules are tightly attached or incorporated into biosilica. Examples are special proteins termed silaffins and long-chain polyamines (LCPAs). Presumably, these biomolecules are involved in the biosilica formation process. Silaffins are highly phosphorylated zwitterions with LCPAs post-translationally attached to lysine residues. In the present work, we use distance-dependent solid-state NMR experiments, especially the 31P{29Si} Rotational Echo Double Resonance (REDOR) technique, to study the environment of phosphate moieties in biosilica and in vitro synthesized SiO2-based composites. In contrast to the heterogeneous mixtures of biomolecules found in native biosilica, the described in vitro silicification experiments make use of a single synthetic phosphopeptide and a LCPA of well-defined and uniform structure. The heteronuclear correlations measured from these silica composites provide reliable 31P-29Si dipolar second moments and information about the distribution of the phosphopeptide within the silica material. The calculated second moment indicates close contact between phosphopeptides and silica. The phosphopeptides are incorporated into the silica composite in a disperse manner. Moreover, the REDOR data acquired for diatom biosilica also imply that phosphate groups are part of the silica-organic interface in this material.
PMID: 32233513 [PubMed - as supplied by publisher]
[NMR paper] PSCD Domains of Pleuralin-1 from the Diatom Cylindrotheca fusiformis: NMR Structures and Interactions with Other Biosilica-Associated Proteins.
PSCD Domains of Pleuralin-1 from the Diatom Cylindrotheca fusiformis: NMR Structures and Interactions with Other Biosilica-Associated Proteins.
PSCD Domains of Pleuralin-1 from the Diatom Cylindrotheca fusiformis: NMR Structures and Interactions with Other Biosilica-Associated Proteins.
Structure. 2016 Jun 14;
Authors: De Sanctis S, Wenzler M, Kröger N, Malloni WM, Sumper M, Deutzmann R, Zadravec P, Brunner E, Kremer W, Kalbitzer HR
Abstract
Diatoms are eukaryotic unicellular algae characterized by silica cell walls and...
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PSCD Domains of Pleuralin-1 from the Diatom Cylindrotheca fusiformis: NMR Structures and Interactions with Other Biosilica-Associated Proteins
PSCD Domains of Pleuralin-1 from the Diatom Cylindrotheca fusiformis: NMR Structures and Interactions with Other Biosilica-Associated Proteins
Publication date: Available online 16 June 2016
Source:Structure</br>
Author(s): Silvia De*Sanctis, Michael Wenzler, Nils Kröger, Wilhelm*M. Malloni, Manfred Sumper, Rainer Deutzmann, Patrick Zadravec, Eike Brunner, Werner Kremer, Hans*Robert Kalbitzer</br>
Diatoms are eukaryotic unicellular algae characterized by silica cell walls and associated with three unique protein families, the pleuralins,...
[NMR paper] Staphylococcus aureus peptidoglycan stem packing by rotational-echo double resonance NMR spectroscopy.
Staphylococcus aureus peptidoglycan stem packing by rotational-echo double resonance NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Staphylococcus aureus peptidoglycan stem packing by rotational-echo double resonance NMR spectroscopy.
Biochemistry. 2013 May 28;52(21):3651-9
Authors: Kim SJ, Singh M, Preobrazhenskaya M, Schaefer J
Abstract
Staphylococcus aureus grown in the presence of an alanine-racemase inhibitor was labeled with d-alanine...
[NMR paper] Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-eno
Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase.
Related Articles Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase.
J Biomol NMR. 2004 Jan;28(1):11-29
Authors: McDowell LM, Poliks B, Studelska DR, O'Connor RD, Beusen DD, Schaefer J
The 46-kD enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the condensation of shikimate-3-phosphate (S3P) and phosphoenolpyruvate to form EPSP....
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[NMR paper] Closed form of liganded glutamine-binding protein by rotational-echo double-resonance
Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR.
Biochemistry. 1997 Aug 5;36(31):9405-8
Authors: Klug CA, Tasaki K, Tjandra N, Ho C, Schaefer J
Rotational-echo double-resonance NMR has been used to determine internuclear distances in the complex of glutamine-binding protein and its ligand, l-glutamine. The...
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[NMR paper] Two-dimensional, rotational-echo double-resonance NMR of cell culture metabolism.
Two-dimensional, rotational-echo double-resonance NMR of cell culture metabolism.
Related Articles Two-dimensional, rotational-echo double-resonance NMR of cell culture metabolism.
J Biol Chem. 1993 Oct 5;268(28):20768-71
Authors: McDowell LM, Cohen ER, Schaefer J
Two-dimensional, rotational-echo double-resonance 13C NMR, a new solid-state NMR technique, has been used to show that the relative fluxes of the labeled chemical bond of L-serine along four metabolic pathways (direct purine synthesis, direct glycine incorporation into protein,...