Expression, Biochemistry, and Stabilization with Camel Antibodies of Membrane Proteins: Case Study of the Mouse 5-HT3 Receptor

2017 ◽  
pp. 139-168 ◽  
Author(s):  
Ghérici Hassaïne ◽  
Cédric Deluz ◽  
Luigino Grasso ◽  
Romain Wyss ◽  
Ruud Hovius ◽  
...  
Keyword(s):  
Membrane Proteins

Thermostabilization of Membrane Proteins by Consensus Mutation: A Case Study for a Fungal Δ8-7 Sterol Isomerase

2020 ◽  
Vol 432 (18) ◽  
pp. 5162-5183 ◽  
Author(s):  
Hebang Yao ◽  
Hongmin Cai ◽  
Dianfan Li
Keyword(s):  
Membrane Proteins ◽  
Consensus Mutation

scholarly journals Integrated in vivo and in vitro nascent chain profiling reveals widespread translational pausing

2016 ◽  
Vol 113 (7) ◽  
pp. E829-E838 ◽  
Author(s):  
Yuhei Chadani ◽  
Tatsuya Niwa ◽  
Shinobu Chiba ◽  
Hideki Taguchi ◽  
Koreaki Ito
Keyword(s):  
Escherichia Coli ◽  
Membrane Proteins ◽  
Ribosome Profiling ◽  
Cytosolic Proteins ◽  
Nascent Polypeptide ◽  
Nascent Chain ◽  
Chemical Trait

Although the importance of the nonuniform progression of elongation in translation is well recognized, there have been few attempts to explore this process by directly profiling nascent polypeptides, the relevant intermediates of translation. Such approaches will be essential to complement other approaches, including ribosome profiling, which is extremely powerful but indirect with respect to the actual translation processes. Here, we use the nascent polypeptide's chemical trait of having a covalently attached tRNA moiety to detect translation intermediates. In a case study,Escherichia coliSecA was shown to undergo nascent polypeptide-dependent translational pauses. We then carried out integrated in vivo and in vitro nascent chain profiling (iNP) to characterize 1,038 proteome members ofE.colithat were encoded by the first quarter of the chromosome with respect to their propensities to accumulate polypeptidyl–tRNA intermediates. A majority of them indeed undergo single or multiple pauses, some occurring only in vitro, some occurring only in vivo, and some occurring both in vivo and in vitro. Thus, translational pausing can be intrinsically robust, subject to in vivo alleviation, or require in vivo reinforcement. Cytosolic and membrane proteins tend to experience different classes of pauses; membrane proteins often pause multiple times in vivo. We also note that the solubility of cytosolic proteins correlates with certain categories of pausing. Translational pausing is widespread and diverse in nature.

scholarly journals Sensitivity of peripheral membrane proteins to the membrane context: A case study of phosphatidylserine and the TIM proteins

2018 ◽  
Vol 1860 (10) ◽  
pp. 2126-2133 ◽  
Author(s):  
Daniel Kerr ◽  
Gregory T. Tietjen ◽  
Zhiliang Gong ◽  
Emad Tajkhorshid ◽  
Erin J. Adams ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Peripheral Membrane Proteins ◽  
Tim Proteins

scholarly journals Probing Membrane Protein Assembly into Nanodiscs by In Situ Dynamic Light Scattering: A2A Receptor as a Case Study

Biology ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 400 ◽  
Author(s):  
Rosana I. Reis ◽  
Isabel Moraes
Keyword(s):  
Light Scattering ◽  
Membrane Proteins ◽  
Dynamic Light Scattering ◽  
Membrane Protein ◽  
Cell Communication ◽  
Cell Physiology ◽  
Functional Characterisation

Membrane proteins play a crucial role in cell physiology by participating in a variety of essential processes such as transport, signal transduction and cell communication. Hence, understanding their structure–function relationship is vital for the improvement of therapeutic treatments. Over the last decade, based on the development of detergents, amphipoles and styrene maleic-acid lipid particles (SMALPs), remarkable accomplishments have been made in the field of membrane protein structural biology. Nevertheless, there are still many drawbacks associated with protein–detergent complexes, depending on the protein in study or experimental application. Recently, newly developed membrane mimetic systems have become very popular for allowing a structural and functional characterisation of membrane proteins in vitro. The nanodisc technology is one such valuable tool, which provides a more native-like membrane environment than detergent micelles or liposomes. In addition, it is also compatible with many biophysical and biochemical methods. Here we describe the use of in situ dynamic light scattering to accurately and rapidly probe membrane proteins’ reconstitution into nanodiscs. The adenosine type 2A receptor (A2AR) was used as a case study.

How to Prepare Membrane Proteins for Solid-State NMR: A Case Study on the α-Helical Integral Membrane Protein Diacylglycerol Kinase from E. coli

ChemBioChem ◽  
2005 ◽  
Vol 6 (9) ◽  
pp. 1693-1700 ◽  
Author(s):  
Mark Lorch ◽  
Salem Faham ◽  
Christoph Kaiser ◽  
Ingrid Weber ◽  
A. James Mason ◽  
...  
Keyword(s):  
Solid State ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Solid State Nmr ◽  
Diacylglycerol Kinase ◽  
Integral Membrane Protein ◽  
E Coli

scholarly journals In silicolocal structure approach: A case study on Outer Membrane Proteins

2008 ◽  
Vol 71 (1) ◽  
pp. 92-109 ◽  
Author(s):  
Juliette Martin ◽  
Alexandre G. de Brevern ◽  
Anne-Claude Camproux
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Structure Approach

scholarly journals Optimizing Conditions for the Isolation of Membrane Proteins by Styrene-Maleic Acid Copolymers: A Case Study on E. Coli Inner Membranes

2017 ◽  
Vol 112 (3) ◽  
pp. 385a
Author(s):  
Jonas M. Doerr ◽  
Martijn C. Koorengevel ◽  
J. Antoinette Killian
Keyword(s):  
Membrane Proteins ◽  
Maleic Acid ◽  
E Coli
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