scholarly journals Protein charge ladders reveal that the net charge of ALS-linked superoxide dismutase can be different in sign and magnitude from predicted values

2014 ◽  
Vol 23 (10) ◽  
pp. 1417-1433 ◽  
Author(s):  
Yunhua Shi ◽  
Alireza Abdolvahabi ◽  
Bryan F. Shaw
Keyword(s):  
Superoxide Dismutase ◽  
Net Charge ◽  
Protein Charge ◽  
Charge Ladders ◽  
Predicted Values

Effects of Cooperativity in Proton Binding on the Net Charge of Proteins in Charge Ladders

2003 ◽  
Vol 107 (19) ◽  
pp. 4653-4666 ◽  
Author(s):  
Upma Sharma ◽  
Russell S. Negin ◽  
Jeffrey D. Carbeck
Keyword(s):  
Net Charge ◽  
Proton Binding ◽  
Charge Ladders

scholarly journals Electrophoresis of Protein Charge Ladders:  A Comparison of Experiment with Various Continuum Primitive Models

2004 ◽  
Vol 108 (14) ◽  
pp. 4516-4524 ◽  
Author(s):  
Stuart A. Allison ◽  
Jeffrey D. Carbeck ◽  
Chuanying Chen ◽  
Felicia Burkes
Keyword(s):  
Protein Charge ◽  
Charge Ladders

scholarly journals To flip or not to flip: lipid–protein charge interactions are a determinant of final membrane protein topology

2008 ◽  
Vol 182 (5) ◽  
pp. 925-935 ◽  
Author(s):  
Mikhail Bogdanov ◽  
Jun Xie ◽  
Phil Heacock ◽  
William Dowhan
Keyword(s):  
Protein Interactions ◽  
Transmembrane Domain ◽  
Lactose Permease ◽  
Membrane Bilayer ◽  
Net Charge ◽  
Protein Charge ◽  
Membrane Protein Topology ◽  
Negative Charge Density ◽  
Lipid Protein Interactions ◽  
Molecular Hinge

The molecular details of how lipids influence final topological organization of membrane proteins are not well understood. Here, we present evidence that final topology is influenced by lipid–protein interactions most likely outside of the translocon. The N-terminal half of Escherichia coli lactose permease (LacY) is inverted with respect to the C-terminal half and the membrane bilayer when assembled in mutants lacking phosphatidylethanolamine and containing only negatively charged phospholipids. We demonstrate that inversion is dependent on interactions between the net charge of the cytoplasmic surface of the N-terminal bundle and the negative charge density of the membrane bilayer surface. A transmembrane domain, acting as a molecular hinge between the two halves of the protein, must also exit from the membrane for inversion to occur. Phosphatidylethanolamine dampens the translocation potential of negative residues in favor of the cytoplasmic retention potential of positive residues, thus explaining the dominance of positive over negative amino acids as co- or post-translational topological determinants.

Evaluating Electrostatic Contributions to Binding with the Use of Protein Charge Ladders

Science ◽  
1996 ◽  
Vol 272 (5261) ◽  
pp. 535-537 ◽  
Author(s):  
J. Gao ◽  
M. Mammen ◽  
G. M. Whitesides
Keyword(s):  
Protein Charge ◽  
Charge Ladders
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