Biophysical characterization of full‐length oleosin in dodecylphosphocholine micelles

2021 ◽  
Author(s):  
Jeffrey A. Julien ◽  
Sarah G. Mutchek ◽  
Nathan J. Wittenberg ◽  
Kerney Jebrell Glover
Keyword(s):  
Full Length ◽  
Biophysical Characterization

scholarly journals Biophysical characterization of the SARS-CoV-2 E protein

2021 ◽  
Author(s):  
Aujan Mehregan ◽  
Sergio Perez-Conesa ◽  
Yuxuan Zhuang ◽  
Ahmad Elbahnsi ◽  
Diletta Pasini ◽  
...  
Keyword(s):  
Recombinant Expression ◽  
Structural Data ◽  
Md Simulations ◽  
Full Length ◽  
Coarse Grained ◽  
Biophysical Characterization ◽  
Viral Budding ◽  
Nmr Structures ◽  
E Protein

SARS-CoV-2 is the virus responsible for the COVID-19 pandemic which continues to wreak havoc across the world, over a year and a half after its effects were first reported in the general media. Current fundamental research efforts largely focus on the SARS-CoV-2 Spike protein. Since successful antiviral therapies are likely to target multiple viral components, there is considerable interest in understanding the biophysical role of its other proteins, in particular structural membrane proteins. Here, we have focused our efforts on the characterization of the full-length E protein from SARS-CoV-2, combining experimental and computational approaches. Recombinant expression of the full-length E protein from SARS-CoV-2 reveals that this membrane protein is capable of independent multimerization, possibly as a tetrameric or smaller species. Fluorescence microscopy shows that the protein localizes intracellularly, and coarse-grained MD simulations indicate it causes bending of the surrounding lipid bilayer, corroborating a potential role for the E protein in viral budding. Although we did not find robust electrophysiological evidence of ion-channel activity, cells transfected with the E protein exhibited reduced intracellular Ca2+, which may further promote viral replication. However, our atomistic MD simulations revealed that previous NMR structures are relatively unstable, and result in models incapable of ion conduction. Our study highlights the importance of using high-resolution structural data obtained from a full-length protein to gain detailed molecular insights, and eventually permitting virtual drug screening.

scholarly journals Structure and biophysical characterization of the human full-length neurturin–GFRa2 complex: A role for heparan sulfate in signaling

2018 ◽  
Vol 293 (15) ◽  
pp. 5492-5508 ◽  
Author(s):  
Jenny Sandmark ◽  
Göran Dahl ◽  
Linda Öster ◽  
Bingze Xu ◽  
Patrik Johansson ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Full Length ◽  
Biophysical Characterization

scholarly journals Biophysical Characterization of Full Length EXOG a Human Mitochondrial Inner Membrane Nuclease

2019 ◽  
Vol 116 (3) ◽  
pp. 76a
Author(s):  
Andrzej B. Dubiel ◽  
Michal R. Szymanski
Keyword(s):  
Full Length ◽  
Inner Membrane ◽  
Biophysical Characterization ◽  
Mitochondrial Inner Membrane

scholarly journals Directed evolution and biophysical characterization of a full-length, soluble, human caveolin-1 variant

2018 ◽  
Vol 1866 (9) ◽  
pp. 963-972
Author(s):  
Joshua N. Smith ◽  
Joshua M. Edgar ◽  
J. Mark Balk ◽  
Mariam Iftikhar ◽  
Jessica C. Fong ◽  
...  
Keyword(s):  
Directed Evolution ◽  
Full Length ◽  
Biophysical Characterization ◽  
Caveolin 1

Biophysical characterization of the interaction between the full-length XIAP and Smac/DIABLO

2021 ◽  
Vol 568 ◽  
pp. 180-185
Author(s):  
Panagis Polykretis ◽  
Enrico Luchinat
Keyword(s):  
Full Length ◽  
Biophysical Characterization

scholarly journals Protein–protein interactions in AQP regulation – biophysical characterization of AQP0–CaM and AQP2–LIP5 complex formation

2018 ◽  
Vol 209 ◽  
pp. 35-54 ◽  
Author(s):  
Stefan Kreida ◽  
Jennifer Virginia Roche ◽  
Caroline Olsson ◽  
Sara Linse ◽  
Susanna Törnroth-Horsefield
Keyword(s):  
Complex Formation ◽  
Protein Interactions ◽  
Full Length ◽  
Regulatory Proteins ◽  
Protein Protein Interactions ◽  
Biophysical Characterization ◽  
Binding Mechanisms

Biophysical characterization of interactions between full-length aquaporins and regulatory proteins provides new insights into binding mechanisms.

scholarly journals Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium

2019 ◽  
Vol 294 (26) ◽  
pp. 10131-10145 ◽  
Author(s):  
Emilia C. Arturo ◽  
Kushol Gupta ◽  
Michael R. Hansen ◽  
Elias Borne ◽  
Eileen K. Jaffe
Keyword(s):  
Quaternary Structure ◽  
Phenylalanine Hydroxylase ◽  
Full Length ◽  
Biophysical Characterization ◽  
Human Phenylalanine Hydroxylase
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