scholarly journals Weak and Transient Protein Interactions Determined by Solid-State NMR

2016 ◽  
Vol 128 (23) ◽  
pp. 6750-6753 ◽  
Author(s):  
Hugh R. W. Dannatt ◽  
Michele Felletti ◽  
Stefan Jehle ◽  
Yao Wang ◽  
Lyndon Emsley ◽  
...  
Keyword(s):  
Solid State ◽  
Protein Interactions ◽  
Solid State Nmr

scholarly journals Solid-State NMR Spectroscopic Study of Chromophore–Protein Interactions in the Pr Ground State of Plant Phytochrome A

2012 ◽  
Vol 5 (3) ◽  
pp. 698-715 ◽  
Author(s):  
Chen Song ◽  
Lars-Oliver Essen ◽  
Wolfgang Gärtner ◽  
Jon Hughes ◽  
Jörg Matysik
Keyword(s):  
Solid State ◽  
Spectroscopic Study ◽  
Protein Interactions ◽  
Ground State ◽  
Solid State Nmr ◽  
Phytochrome A

scholarly journals MAS NMR on a Red/Far-Red Photochromic Cyanobacteriochrome All2699 from Nostoc

2019 ◽  
Vol 20 (15) ◽  
pp. 3656 ◽  
Author(s):  
Qian-Zhao Xu ◽  
Pavlo Bielytskyi ◽  
James Otis ◽  
Christina Lang ◽  
Jon Hughes ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Solid State ◽  
Spectroscopic Study ◽  
Protein Interactions ◽  
Solid State Nmr ◽  
Structural Model ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Dark State ◽  
Stabilizing Element

Unlike canonical phytochromes, the GAF domain of cyanobacteriochromes (CBCRs) can bind bilins autonomously and is sufficient for functional photocycles. Despite the astonishing spectral diversity of CBCRs, the GAF1 domain of the three-GAF-domain photoreceptor all2699 from the cyanobacterium Nostoc 7120 is the only CBCR-GAF known that converts from a red-absorbing (Pr) dark state to a far-red-absorbing (Pfr) photoproduct, analogous to the more conservative phytochromes. Here we report a solid-state NMR spectroscopic study of all2699g1 in its Pr state. Conclusive NMR evidence unveils a particular stereochemical heterogeneity at the tetrahedral C31 atom, whereas the crystal structure shows exclusively the R-stereochemistry at this chiral center. Additional NMR experiments were performed on a construct comprising the GAF1 and GAF2 domains of all2699, showing a greater precision in the chromophore–protein interactions in the GAF1-2 construct. A 3D Pr structural model of the all2699g1-2 construct predicts a tongue-like region extending from the GAF2 domain (akin to canonical phytochromes) in the direction of the chromophore, shielding it from the solvent. In addition, this stabilizing element allows exclusively the R-stereochemistry for the chromophore-protein linkage. Site-directed mutagenesis performed on three conserved motifs in the hairpin-like tip confirms the interaction of the tongue region with the GAF1-bound chromophore.

scholarly journals Weak and Transient Protein Interactions Determined by Solid-State NMR

2016 ◽  
Vol 55 (23) ◽  
pp. 6638-6641 ◽  
Author(s):  
Hugh R. W. Dannatt ◽  
Michele Felletti ◽  
Stefan Jehle ◽  
Yao Wang ◽  
Lyndon Emsley ◽  
...  
Keyword(s):  
Solid State ◽  
Protein Interactions ◽  
Solid State Nmr

Lysine-Capped Silica Nanoparticles: A Solid-State NMR Spectroscopy Study

MRS Advances ◽  
2016 ◽  
Vol 1 (31) ◽  
pp. 2261-2266 ◽  
Author(s):  
Chengchen Guo ◽  
Gregory P. Holland ◽  
Jeffery L. Yarger
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Silica Nanoparticles ◽  
Protein Interactions ◽  
Solid State Nmr ◽  
Silanol Group ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Solid State Nmr Spectroscopy ◽  
Fumed Silica Nanoparticles

ABSTRACTTo achieve the goal of biocompatibility in nano-based materials we must first obtain a fundamental understanding of the physical and chemical behavior of biomolecules at the interfaces of nanomaterials. A first step towards understanding protein interactions with nanomaterials is to understand how individual amino acids interact at the interfaces. In this paper, we investigated the lysine adsorption behavior on fumed silica nanoparticles by solid-state NMR spectroscopy. We use 1H, 13C and 15N solid-state magic angle spinning (MAS) NMR techniques to elucidate how lysine is adsorbed on silica nanoparticles surfaces via strong hydrogen-bonding interaction between the protonated side-chain amine group and silanol group on silica nanoparticles surfaces.*

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