JMS/sandbox15: Difference between revisions

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Another way to say this, in the case of proteins <scene name='57/575026/Electrostatics/16'>in solvents such as water</scene>, is that, for each and every protein, <scene name='57/575026/Electrostatics/24'>water binds to the hydrogens</scene> (e.g., lysine's ammonium at physiology pH has three hydrogens - not shown) coming off a positively charged atom, or associates with the charged atom itself, thus screening each protein from the other proteins.  
Another way to say this, in the case of proteins <scene name='57/575026/Electrostatics/16'>in solvents such as water</scene>, is that, for each and every protein, <scene name='57/575026/Electrostatics/24'>water binds to the hydrogens</scene> (e.g., lysine's ammonium at physiology pH has three hydrogens - not shown) coming off a positively charged atom, or associates with the charged atom itself, thus screening each protein from the other proteins.  


Still, this picture is incomplete. While illustrative of the basic principles of how small electrostatic fields changes can greatly increase a protein's solubility, there other contributing factors to the electrostatic field, e.g.,  solvated ions, crowding conditions, and the neighboring residues to these divergent residues. For example, when a negatively charged residue neigbors one of these additional positive residues, then from a distance relatively larger than the distance between the two oppositely charged residues, the electrostatic field is zero.
Still, this picture is incomplete. While illustrative of the basic principles of how small electrostatic fields changes can greatly increase a protein's solubility, there other contributing factors to the electrostatic field, e.g.,  solvated ions, crowding conditions, and the neighboring residues to these divergent residues. For example, when a negatively charged residue neigbors one of these additional positive residues, then from a distance relatively larger than the distance between the two oppositely charged residues, the electrostatic field is zero<ref>https://pdb101.rcsb.org/motm/1#:~:text=PDB%2D101%3A%20Molecule%20of%20the%20Month%3A%20Myoglobin.</ref>


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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Joseph M. Steinberger