scholarly journals Methyl-Specific Isotope Labeling Strategies for NMR Studies of Membrane Proteins

2017 ◽  
pp. 109-123 ◽  
Author(s):  
Vilius Kurauskas ◽  
Paul Schanda ◽  
Remy Sounier
Keyword(s):  
Membrane Proteins ◽  
Isotope Labeling ◽  
Nmr Studies ◽  
Labeling Strategies

scholarly journals Isotope labeling strategies for NMR studies of RNA

2009 ◽  
Vol 46 (1) ◽  
pp. 113-125 ◽  
Author(s):  
Kun Lu ◽  
Yasuyuki Miyazaki ◽  
Michael F. Summers
Keyword(s):  
Isotope Labeling ◽  
Nmr Studies ◽  
Labeling Strategies

Isotope Labeling Strategies for Analysis of an Ion Channel Cytoplasmic Domain by NMR Spectroscopy

2013 ◽  
pp. 289-300
Author(s):  
Karin Abarca-Heidemann ◽  
Elke Duchardt-Ferner ◽  
Jens Woehnert ◽  
Brad S. Rothberg
Keyword(s):  
Nmr Spectroscopy ◽  
Ion Channel ◽  
Isotope Labeling ◽  
Cytoplasmic Domain ◽  
Labeling Strategies

Synthetic Biology-Based Solution NMR Studies on Membrane Proteins in Lipid Environments

2019 ◽  
pp. 143-185 ◽  
Author(s):  
Erik Henrich ◽  
Frank Löhr ◽  
Julija Mezhyrova ◽  
Aisha Laguerre ◽  
Frank Bernhard ◽  
...  
Keyword(s):  
Synthetic Biology ◽  
Membrane Proteins ◽  
Solution Nmr ◽  
Nmr Studies

Lipid−Protein Nanodiscs as Reference Medium in Detergent Screening for High-Resolution NMR Studies of Integral Membrane Proteins

2010 ◽  
Vol 132 (16) ◽  
pp. 5628-5629 ◽  
Author(s):  
Zakhar O. Shenkarev ◽  
Ekaterina N. Lyukmanova ◽  
Alexander S. Paramonov ◽  
Lyudmila N. Shingarova ◽  
Vladimir V. Chupin ◽  
...  
Keyword(s):  
High Resolution ◽  
Membrane Proteins ◽  
Integral Membrane Proteins ◽  
Nmr Studies ◽  
High Resolution Nmr ◽  
Reference Medium

scholarly journals Monitoring mitochondrial translation by pulse SILAC

2021 ◽  
Author(s):  
Koshi Imami ◽  
Matthias Selbach ◽  
Yasushi Ishihama
Keyword(s):  
Oxidative Stress ◽  
Amino Acids ◽  
Membrane Proteins ◽  
Translational Regulation ◽  
Isotope Labeling ◽  
Protein Complexes ◽  
Complex Iii ◽  
Mitochondrial Translation ◽  
Mitochondrial Ribosomes ◽  
Hydrophobic Nature

SummaryMitochondrial ribosomes are specialized to translate the 13 membrane proteins encoded in the mitochondrial genome, but it is challenging to quantify mitochondrial translation products due to their hydrophobic nature. Here, we introduce a proteomic method that combines biochemical isolation of mitochondria with pulse stable isotope labeling by amino acids in cell culture (pSILAC). Our method provides the highest protein coverage (quantifying 12 out of the 13 inner-membrane proteins; average 2-fold improvement over previous studies) with the shortest measurement time. We applied this method to uncover the global picture of (post)translational regulation of both mitochondrial- and nuclear-encoded proteins involved in the assembly of protein complexes that mediate oxidative phosphorylation (OXPHOS). The results allow us to infer the assembly order of complex components and/or partners, as exemplified by complex III. This method should be applicable to study mitochondrial translation programs in many contexts, including oxidative stress and mitochondrial disease.

scholarly journals Understanding GPCR recognition and folding from NMR studies of fragments

RSC Advances ◽  
2018 ◽  
Vol 8 (18) ◽  
pp. 9858-9870 ◽  
Author(s):  
Jacopo Marino ◽  
Reto Walser ◽  
Martin Poms ◽  
Oliver Zerbe
Keyword(s):  
Protein Folding ◽  
Membrane Proteins ◽  
Membrane Insertion ◽  
Nmr Studies

Cotranslational protein folding is a vectorial process, and for membrane proteins, N-terminal helical segments are the first that become available for membrane insertion. Here fragments corresponding to these segments are investigated by NMR.

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