Photosynthetic light-harvesting complexes have a remarkable capacity to perform robust photo-physics at ambient temperatures and in fluctuating environments. Protein conformational dynamics and membrane mobility are processes that contribute to the light-harvesting efficiencies and control photoprotective responses. This short review describes the application of magic angle spinning nuclear magnetic resonance (NMR) spectroscopy for characterizing the structural dynamics of pigment, protein, and...
[NMR paper] Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR.
Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR.
Related Articles Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR.
Methods. 2018 Apr 24;:
Authors: Matlahov I, van der Wel PCA
Abstract
Solid-state nuclear magnetic resonance (ssNMR) spectroscopy enables the structural characterization of a diverse array of biological assemblies that include amyloid fibrils, non-amyloid aggregates, membrane-associated proteins and viral capsids....
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04-28-2018 03:16 PM
Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR
Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR
Publication date: December 2016
Source:Biochimica et Biophysica Acta (BBA) - Bioenergetics, Volume 1857, Issue 12</br>
Author(s): Fatemeh Azadi Chegeni, Giorgio Perin, Karthick Babu Sai Sankar Gupta, Diana Simionato, Tomas Morosinotto, Anjali Pandit</br>
Photosynthetic thylakoid membranes contain the protein machinery to convert sunlight in chemical energy and regulate this process in changing environmental conditions via interplay between lipid,...
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09-22-2016 06:33 AM
[NMR paper] Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR.
Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR.
Biochim Biophys Acta. 2016 Sep 11;
Authors: Chegeni FA, Perin G, Gupta KB, Simionato D, Morosinotto T, Pandit A
Abstract
Photosynthetic thylakoid membranes contain the protein...
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09-22-2016 06:31 AM
[NMR paper] Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.
Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.
Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.
Solid State Nucl Magn Reson. 2015 Sep 14;
Authors: Williams JK, Schmidt-Rohr K, Hong M
Abstract
The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping (13)C chemical shift ranges between 100 and 160ppm,...
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10-07-2015 11:27 AM
Aromatic spectral editing Techniques for magic-Angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins
Aromatic spectral editing Techniques for magic-Angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins
Publication date: Available online 14 September 2015
Source:Solid State Nuclear Magnetic Resonance</br>
Author(s): Jonathan K. Williams, Klaus Schmidt-Rohr, Mei Hong</br>
The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, give highly overlapped 13C chemical shifts between 100 and 160ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet...
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09-14-2015 10:42 PM
[NMR paper] Structural Dynamics and Conformational Equilibria of SERCA Regulatory Proteins in Membranes by Solid-State NMR Restrained Simulations.
Structural Dynamics and Conformational Equilibria of SERCA Regulatory Proteins in Membranes by Solid-State NMR Restrained Simulations.
Related Articles Structural Dynamics and Conformational Equilibria of SERCA Regulatory Proteins in Membranes by Solid-State NMR Restrained Simulations.
Biophys J. 2014 Jun 17;106(12):2566-2576
Authors: De Simone A, Mote KR, Veglia G
Abstract
Solid-state NMR spectroscopy is emerging as a powerful approach to determine structure, topology, and conformational dynamics of membrane proteins at the...
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06-19-2014 06:59 PM
Structural Dynamics and Conformational Equilibria of SERCA Regulatory Proteins in Membranes by Solid-State NMR Restrained Simulations
Structural Dynamics and Conformational Equilibria of SERCA Regulatory Proteins in Membranes by Solid-State NMR Restrained Simulations
Publication date: 17 June 2014
Source:Biophysical Journal, Volume 106, Issue 12</br>
Author(s): Alfonso De*Simone , Kaustubh*R. Mote , Gianluigi Veglia</br>
Solid-state NMR spectroscopy is emerging as a powerful approach to determine structure, topology, and conformational dynamics of membrane proteins at the atomic level. Conformational dynamics are often inferred and quantified from the motional averaging of the NMR parameters....
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06-18-2014 06:09 PM
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Photosynth Res. 2011 Aug 13;
Authors: Pandit A, de Groot HJ
This short review describes how solid-state NMR has provided a mechanistic and electronic picture of pigment-protein and pigment-pigment interactions in photosynthetic antenna complexes. NMR results on purple bacterial antenna complexes show how the packing of the protein and the pigments inside the light-harvesting oligomers induces mutual...
Structural dynamics of light harvesting proteins, photosynthetic membranes, and cells observed by spectral editing solid-state NMR
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