Measurement of Electrostatic Interactions in Protein Folding with the Use of Protein Charge Ladders

2002 ◽  
Vol 124 (12) ◽  
pp. 2911-2916 ◽  
Author(s):  
Russell S. Negin ◽  
Jeffrey D. Carbeck
Keyword(s):  
Protein Folding ◽  
Electrostatic Interactions ◽  
Protein Charge ◽  
Charge Ladders

Globular–disorder transition in proteins: a compromise between hydrophobic and electrostatic interactions?

2016 ◽  
Vol 18 (33) ◽  
pp. 23207-23214 ◽  
Author(s):  
Anupaul Baruah ◽  
Parbati Biswas
Keyword(s):  
Protein Folding ◽  
Electrostatic Interactions ◽  
Protein Disorder ◽  
Disorder Transition ◽  
P Protein

Protein disorder, like protein folding, satisfies the principle of minimal frustration.

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

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

Protein folds: towards understanding folding from inspection of native structures

1995 ◽  
Vol 348 (1323) ◽  
pp. 71-79 ◽  
Keyword(s):  
Protein Folding ◽  
Protein Structure ◽  
Secondary Structure ◽  
Electrostatic Interactions ◽  
Protein Domain ◽  
Major Influence ◽  
Protein Topology ◽  
Protein Folds ◽  
Short Summary ◽  
Folded Proteins

Following a short summary of some of the principal features of folded proteins, the results of two complementary studies of protein structure are presented, the first concerned with the factors which influence secondary structure propensity and the second an analysis of protein topology. In an attempt to deconvolute the physical contributions to secondary structure propensities, we have calculated intrinsic ɸ,ψ propensities, derived from the coil regions of proteins. Comparison of intrinsic ɸ,ψ propensities with their equivalent secondary structure values show correlations for both helix and strand. This suggests that the local dipeptide, steric and electrostatic interactions have a major influence on secondary structure propensity. We then proceed to inspect the distribution of protein domain folds observed to date. Several folds occur very commonly, so that 46% of the current non-homologous database comprises only nine folds. The implications of these results for protein folding are discussed.

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