Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: molecular dynamics calculations

2000 ◽  
Vol 302 (3) ◽  
pp. 727-746 ◽  
Author(s):  
Horia I Petrache ◽  
Alan Grossfield ◽  
Kevin R MacKenzie ◽  
Donald M Engelman ◽  
Thomas B Woolf
Biochemistry ◽  
2006 ◽  
Vol 45 (48) ◽  
pp. 14298-14310 ◽  
Author(s):  
Jonathan M. Cuthbertson ◽  
Peter J. Bond ◽  
Mark S. P. Sansom

Author(s):  
S. Kirchanski ◽  
D. Branton

We have investigated the effect of integral membrane proteins upon the fracturing of frozen lipid bilayers. This investigation has been part of an effort to develop freeze fracture labeling techniques and to assess the possible breakage of covalent protein bonds during the freeze fracture process. We have developed an experimental protocol utilizing lectin affinity columns which should detect small amounts of covalent bond breakage during the fracture of liposomes containing purified (1) glycophorin (a transmembrane glycoprotein of human erythrocyte membranes). To fracture liposomes in bulk, frozen liposomes are ground repeatedly under liquid nitrogen. Failure to detect any significant covalent bond breakage (contrary to (2)) led us to question the effectiveness of our grinding procedure in fracturing and splitting lipid bilayers.


2005 ◽  
Vol 15 (4) ◽  
pp. 413-422 ◽  
Author(s):  
Michael M. Micci ◽  
S. J. Lee ◽  
B. Vieille ◽  
C. Chauveau ◽  
Iskendar Gokalp

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