Charged Gels as Orienting Media for Measurement of Residual Dipolar Couplings in Soluble and Integral Membrane Proteins

2004 ◽  
Vol 126 (49) ◽  
pp. 16259-16266 ◽  
Author(s):  
Tomasz Cierpicki ◽  
John H. Bushweller
2009 ◽  
Vol 131 (40) ◽  
pp. 14140-14141 ◽  
Author(s):  
Sang Ho Park ◽  
Woo Sung Son ◽  
Rishi Mukhopadhyay ◽  
Homayoun Valafar ◽  
Stanley J. Opella

Author(s):  
D.J. Benefiel ◽  
R.S. Weinstein

Intramembrane particles (IMP or MAP) are components of most biomembranes. They are visualized by freeze-fracture electron microscopy, and they probably represent replicas of integral membrane proteins. The presence of MAP in biomembranes has been extensively investigated but their detailed ultrastructure has been largely ignored. In this study, we have attempted to lay groundwork for a systematic evaluation of MAP ultrastructure. Using mathematical modeling methods, we have simulated the electron optical appearances of idealized globular proteins as they might be expected to appear in replicas under defined conditions. By comparing these images with the apearances of MAPs in replicas, we have attempted to evaluate dimensional and shape distortions that may be introduced by the freeze-fracture technique and further to deduce the actual shapes of integral membrane proteins from their freezefracture images.


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