scholarly journals From polymer chemistry to structural biology: The development of SMA and related amphipathic polymers for membrane protein extraction and solubilisation

2019 ◽  
Vol 221 ◽  
pp. 167-175 ◽  
Author(s):  
Juan Francisco Bada Juarez ◽  
Andrew J. Harper ◽  
Peter J. Judge ◽  
Stephen R. Tonge ◽  
Anthony Watts
Author(s):  
Thi Kim Hoang Trinh ◽  
Weihua Qiu ◽  
Meg Thornton ◽  
Everett E. Carpenter ◽  
Youzhong Guo

2008 ◽  
Vol 130 (23) ◽  
pp. 7357-7363 ◽  
Author(s):  
Qinghai Zhang ◽  
Reto Horst ◽  
Michael Geralt ◽  
Xingquan Ma ◽  
Wen-Xu Hong ◽  
...  

2003 ◽  
Vol 2003 (4) ◽  
pp. 249-255 ◽  
Author(s):  
M. Walid Qoronfleh ◽  
Betsy Benton ◽  
Ray Ignacio ◽  
Barbara Kaboord

The human proteome project will demand faster, easier, and more reliable methods to isolate and purify protein targets. Membrane proteins are the most valuable group of proteins since they are the target for 70–80% of all drugs. Perbio Science has developed a protocol for the quick, easy, and reproducible isolation of integral membrane proteins from eukaryotic cells. This procedure utilizes a proprietary formulation to facilitate cell membrane disruption in a mild, nondenaturing environment and efficiently solubilizes membrane proteins. The technique utilizes a two-phase partitioning system that enables the class separation of hydrophobic and hydrophilic proteins. A variety of protein markers were used to investigate the partitioning efficiency of the membrane protein extraction reagents (Mem-PER) (Mem-PER is a registered trademark of Pierce Biotechnology, Inc) system. These included membrane proteins with one or more transmembrane spanning domains as well as peripheral and cytosolic proteins. Based on densitometry analyses of our Western blots, we obtained excellent solubilization of membrane proteins with less than 10% contamination of the hydrophobic fraction with hydrophilic proteins. Compared to other methodologies for membrane protein solubilization that use time-consuming protocols or expensive and cumbersome instrumentation, the Mem-PER reagents system for eukaryotic membrane protein extraction offers an easy, efficient, and reproducible method to isolate membrane proteins from mammalian and yeast cells.


2015 ◽  
Vol 33 ◽  
pp. 115-125 ◽  
Author(s):  
Richard Neutze ◽  
Gisela Brändén ◽  
Gebhard FX Schertler

Biology ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 401
Author(s):  
James Birch ◽  
Harish Cheruvara ◽  
Nadisha Gamage ◽  
Peter J. Harrison ◽  
Ryan Lithgo ◽  
...  

Membrane proteins are essential components of many biochemical processes and are important pharmaceutical targets. Membrane protein structural biology provides the molecular rationale for these biochemical process as well as being a highly useful tool for drug discovery. Unfortunately, membrane protein structural biology is a difficult area of study due to low protein yields and high levels of instability especially when membrane proteins are removed from their native environments. Despite this instability, membrane protein structural biology has made great leaps over the last fifteen years. Today, the landscape is almost unrecognisable. The numbers of available atomic resolution structures have increased 10-fold though advances in crystallography and more recently by cryo-electron microscopy. These advances in structural biology were achieved through the efforts of many researchers around the world as well as initiatives such as the Membrane Protein Laboratory (MPL) at Diamond Light Source. The MPL has helped, provided access to and contributed to advances in protein production, sample preparation and data collection. Together, these advances have enabled higher resolution structures, from less material, at a greater rate, from a more diverse range of membrane protein targets. Despite this success, significant challenges remain. Here, we review the progress made and highlight current and future challenges that will be overcome.


Methods ◽  
2011 ◽  
Vol 55 (4) ◽  
pp. 318-323 ◽  
Author(s):  
Qinghai Zhang ◽  
Houchao Tao ◽  
Wen-Xu Hong

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