Electrostatic aspects of protein-protein interactions.

By F. Sheinerman, Raquel Norel, Barry Honig. Current Opinion in Structural Biology, 2000

724 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/668e68de3c3bbd4d589feb9db730b3370624b949

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Citations in the corpus

Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. (2005, background): “In some cases, however, polar and charged interactions can contribute significantly to the binding energy (Sheinerman et al., 2000).”
Analysing six types of protein-protein interfaces. (2003, background): “A few groups found polar and charged residues as well as saltbridges to be the major contributors for the formation of interactions.(11,17,22) Other studies reported that salt-bridges are not an important factor in protein–protein interaction,(9) or that interfaces favour non-polar residues.”
Protein–protein interaction and quaternary structure (2008, background): “Electrostatics plays an essential role in all processes involving proteins, DNA or RNA, but its evaluation requires elaborate calculations that are highly sensitive to the solvent model (Sheinerman et al. 2000).”
The Poisson–Boltzmann equation for biomolecular electrostatics: a tool for structural biology (2002, background): “A general principle is that networks of interactions, rather than single interactions, are required to balance desolvation energies.”
Recent progress and future directions in protein-protein docking. (2008, background): “However, the bulky side chains of Trp, Arg, and Tyr appear in hot spots with high frequencies (21%, 13%, and 12%, respectively), whereas Leu, Met, Ser, Thr, and Val residues are rarely observed in hot spots (3% frequency or less) [72].”
An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes. (2003, background): “Experimental as well as theoretical studies have highlighted the role of electrostatic interactions in determining the rate of association of protein– protein complexes,(40) as well as for recognition specificity.(41) While the role of hydrogen bonds and charge–charge interactions for specificity ap”
Demystifying Heparan Sulfate–Protein Interactions (2014, background): “Second, electrostatic interactions to a large extent drive the interaction between HSBPs and HS, which allows fast absorption of protein from the soluble phase (31, 32).”
ASEdb: a database of alanine mutations and their effects on the free energy of binding in protein interactions (2001, methodology): “This data has also been used to study solvent (Janin, 1999), electrostatics (Sheinerman et al., 2000), and evolutionary conservation (Hu et al.”
H++: a server for estimating pKas and adding missing hydrogens to macromolecules (2005, background): “Electrostatic interactions are often a key factor determining the properties of biomolecules (1–5), including their biological function such as catalytic activity (6,7), ligand binding (8), complex formation (9) and proton transport (10), as well as their structure and stability (11,12).”
Protein-Protein Interactions: Coupling of Structurally Conserved Residues and of Hot Spots across Interfaces. Implications for Docking (2004, background): “Nevertheless, while not observed statistically overall, electrostatic interactions and hydrogen bonds are well known to be crucial to the stability of protein-protein complexes (Sheinerman et al., 2000; Norel et al., 2001; Fernandez and Scheraga, 2003).”
The intrinsic contributions of tyrosine, serine, glycine and arginine to the affinity and specificity of antibodies. (2008, background): “In contrast, it is generally believed that Arg and other charged residues contribute specificity to molecular recognition by establishing precise electrostatic and hydrogen-bonding interactions.(39) Our results clearly show that Tyr residues combined with flexible Ser/Gly residues are capable of med”