Patterns formed by protein reactions and diffusion are the foundation for many phenomena in biology. Yet, the experimental study of reaction-diffusion (R-D) systems has so far been dominated by chemical oscillators, for which many manipulation tools are available. Here, we developed a photoswitch for the Min system of Escherichia coli, a versatile biological in vitro R-D system consisting of the antagonistic proteins MinD and MinE. A MinE-derived peptide of 19 amino acids is covalently modified with a photoisomerizable crosslinker based on azobenzene to externally control peptide-mediated depletion of MinD from the membrane. In addition to providing an on-off switch for pattern formation, we achieve frequency-locked entrainment with a precise 2D spatial memory, allowing new insights into Min protein action on the membrane. Taken together, we provide a tool to externally control protein patterns formed by self-organization.
[NMR paper] Characterization of conjugation pattern in large polysaccharide-protein conjugates by NMR.
Characterization of conjugation pattern in large polysaccharide-protein conjugates by NMR.
Related Articles Characterization of conjugation pattern in large polysaccharide-protein conjugates by NMR.
Angew Chem Int Ed Engl. 2017 Oct 10;:
Authors: Giuntini S, Balducci E, Cerofolini L, Ravera E, Fragai M, Berti F, Luchinat C
Abstract
Carbohydrate-based vaccines are among the safest and most effective vaccines and represent potent tools for prevention of life-threatening bacterial infectious diseases, like meningitis and pneumonia....
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10-14-2017 02:04 AM
[NMR paper] Characterization of conjugation pattern in large polysaccharide-protein conjugates by NMR
Characterization of conjugation pattern in large polysaccharide-protein conjugates by NMR
Carbohydrate-based vaccines are among the safest and most effective vaccines and represent potent tools for prevention of life-threatening bacterial infectious diseases, like meningitis and pneumonia. The chemical conjugation of a weak antigen to protein as a source of T-cell epitopes generates a glycoconjugate vaccine, that results more immunogenic. Several methods have been used so far to characterize the resulting polysaccharide-protein conjugates. However, a reduced number of methodologies has...
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10-10-2017 09:37 PM
Disulfide Bond Pattern of Transforming Growth Factor ?-Induced Protein
Disulfide Bond Pattern of Transforming Growth Factor ?-Induced Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00694/20160922/images/medium/bi-2016-006945_0011.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00694
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/H99XLbDTxLw
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[NMR paper] NMR analysis of the acetylation pattern of the neuronal Tau protein.
NMR analysis of the acetylation pattern of the neuronal Tau protein.
NMR analysis of the acetylation pattern of the neuronal Tau protein.
Biochemistry. 2014 Apr 7;
Authors: Kamah A, Huvent I, Cantrelle FX, Qi H, Lippens G, Landrieu I, Smet-Nocca C
Abstract
Lysine acetylation of the neuronal Tau protein was described as a novel mechanism of posttranslational regulation of Tau functions with important outcomes in microtubule binding and aggregation processes related to Alzheimer's disease. Here, we unravel at a per-residue...
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04-09-2014 10:40 AM
Proton polarization in photo-excited aromatic molecule at room temperature enhanced by intense optical source and temperature control
From The DNP-NMR Blog:
Proton polarization in photo-excited aromatic molecule at room temperature enhanced by intense optical source and temperature control
Sakaguchi, S., et al., Proton polarization in photo-excited aromatic molecule at room temperature enhanced by intense optical source and temperature control. Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms, 2013. 317(0): p. 679-684.
http://www.sciencedirect.com/science/article/pii/S0168583X13008872
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01-23-2014 01:37 AM
Proton polarization in photo-excited aromatic molecule at room temperature enhanced by intense optical source and temperature control
From The DNP-NMR Blog:
Proton polarization in photo-excited aromatic molecule at room temperature enhanced by intense optical source and temperature control
Sakaguchi, S., et al., Proton polarization in photo-excited aromatic molecule at room temperature enhanced by intense optical source and temperature control. Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms, 2013(0).
http://www.sciencedirect.com/science/article/pii/S0168583X13008872
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11-21-2013 01:14 AM
[NMR paper] Insights into tyrosine phosphorylation control of protein-protein association from th
Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase.
Related Articles Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase.
Biochemistry. 1998 Jan 20;37(3):867-77
Authors: Eisenmesser EZ, Post CB
A protein-protein association regulated by phosphorylation of tyrosine is examined by NMR...
Optical control of protein pattern formation
Linear Mode
