[NMR paper] A Dynamic Equilibrium of Three Hydrogen-Bond Conformers Explains the NMR Spectrum of the Active Site of Photoactive Yellow Protein.
A Dynamic Equilibrium of Three Hydrogen-Bond Conformers Explains the NMR Spectrum of the Active Site of Photoactive Yellow Protein.
Related Articles A Dynamic Equilibrium of Three Hydrogen-Bond Conformers Explains the NMR Spectrum of the Active Site of Photoactive Yellow Protein.
J Chem Theory Comput. 2016 Sep 14;
Authors: Taenzler PJ, Sadeghian K, Ochsenfeld C
Abstract
A theoretical study on the NMR shifts of the hydrogen bond network around the chromophore, para-coumaric acid (pCA), of photoactive yellow protein (PYP) is...
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09-22-2016 06:31 AM
[NMR paper] Theoretical analysis of geometry and NMR isotope shift in hydrogen-bonding center of photoactive yellow protein by combination of multicomponent quantum mechanics and ONIOM scheme.
Theoretical analysis of geometry and NMR isotope shift in hydrogen-bonding center of photoactive yellow protein by combination of multicomponent quantum mechanics and ONIOM scheme.
Theoretical analysis of geometry and NMR isotope shift in hydrogen-bonding center of photoactive yellow protein by combination of multicomponent quantum mechanics and ONIOM scheme.
J Chem Phys. 2014 Nov 14;141(18):185101
Authors: Kanematsu Y, Tachikawa M
Abstract
Multicomponent quantum mechanical (MC_QM) calculation has been extended with ONIOM (our...
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11-17-2014 12:48 PM
The EF Loop in Green Proteorhodopsin Affects Conformation and*Photocycle dynamics
From The DNP-NMR Blog:
The EF Loop in Green Proteorhodopsin Affects Conformation and*Photocycle dynamics
Mehler, M., et al., The EF Loop in Green Proteorhodopsin Affects Conformation and Photocycle dynamics. Biophysical Journal, 2013. 105(2): p. 385-397.
http://dx.doi.org/10.1016/j.bpj.2013.06.014
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08-16-2013 08:36 PM
Comprehensive Determination of Protein Tyrosine pKa Values for Photoactive Yellow Protein Using Indirect 13C NMR Spectroscopy
Comprehensive Determination of Protein Tyrosine pKa Values for Photoactive Yellow Protein Using Indirect 13C NMR Spectroscopy
8 February 2012
Publication year: 2012
Source:Biophysical Journal, Volume 102, Issue 3</br>
</br>
Upon blue-light irradiation, the bacterium Halorhodospira halophila is able to modulate the activity of its flagellar motor and thereby evade potentially harmful UV radiation. The 14*kDa soluble cytosolic photoactive yellow protein (PYP) is believed to be the primary mediator of this photophobic response, and yields a UV/Vis absorption spectrum that...
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02-03-2013 10:13 AM
Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins
Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins
Abstract The solution NMR resonance assignment of the protein backbone is most commonly carried out using triple resonance experiments that involve 15N and 1HN resonances. The assignment becomes problematic when there is resonance overlap of 15Nâ??1HN cross peaks. For such residues, one cannot unambiguously link the â??leftâ?? side of the NH root to the â??rightâ?? side, and the residues associated with such overlapping HN resonances remain often unassigned. Here we present a...
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12-31-2010 08:38 PM
[NMR paper] Molecular dynamics simulations of photoactive yellow protein (PYP) in three states of
Molecular dynamics simulations of photoactive yellow protein (PYP) in three states of its photocycle: a comparison with X-ray and NMR data and analysis of the effects of Glu46 deprotonation and mutation.
Related Articles Molecular dynamics simulations of photoactive yellow protein (PYP) in three states of its photocycle: a comparison with X-ray and NMR data and analysis of the effects of Glu46 deprotonation and mutation.
Eur Biophys J. 2002 Dec;31(7):504-20
Authors: Antes I, Thiel W, van Gunsteren WF
Photoactive yellow protein (PYP) is a...
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11-24-2010 08:58 PM
[NMR paper] Probing the nature of the blue-shifted intermediate of photoactive yellow protein in
Probing the nature of the blue-shifted intermediate of photoactive yellow protein in solution by NMR: hydrogen-deuterium exchange data and pH studies.
Related Articles Probing the nature of the blue-shifted intermediate of photoactive yellow protein in solution by NMR: hydrogen-deuterium exchange data and pH studies.
Biochemistry. 2000 Nov 28;39(47):14392-9
Authors: Craven CJ, Derix NM, Hendriks J, Boelens R, Hellingwerf KJ, Kaptein R
The nature of the pB intermediate of photoactive yellow protein (PYP) from Ectothiorhodospira halophila has...
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11-19-2010 08:29 PM
[NMR paper] Early and late M intermediates in the bacteriorhodopsin photocycle: a solid-state NMR
Early and late M intermediates in the bacteriorhodopsin photocycle: a solid-state NMR study.
Related Articles Early and late M intermediates in the bacteriorhodopsin photocycle: a solid-state NMR study.
Biochemistry. 1998 Jun 2;37(22):8088-96
Authors: Hu JG, Sun BQ, Bizounok M, Hatcher ME, Lansing JC, Raap J, Verdegem PJ, Lugtenburg J, Griffin RG, Herzfeld J
To enforce vectorial proton transport in bacteriorhodopsin (bR), it is necessary that there be a change in molecular structure between deprotonation and reprotonation of the...