/biz/ - Business & Finance

>>16796986
Tubulin, like other proteins, is composed of a heterogeneous group of amino acid residues connected to peptide backbones. The residues include both water-soluble polar, and water-insoluble non-polar groups, the latter including ‘aromatic’ amino acids (phenylalanine, tyrosine and tryptophan) with ‘π’ orbital electron resonance clouds in phenyl and indole rings. π orbital clouds are composed of electrons able to delocalize across a spatial region. Like oil separating from water, non-polar electron clouds coalesce during protein folding to form isolated water-excluding ‘hydrophobic regions’ within proteins with particular (‘oily’, ‘lipid-like’) solubility. Driving the folding are non-polar, but highly polarizable π orbital electron cloud dipoles which couple by van der Waals London forces (instantaneous dipole-induced dipole attractions between electron clouds) [78].

>Driving the folding are non-polar, but highly polarizable π orbital electron cloud dipoles which couple by van der Waals London forces

>>16753292
>electron pi orbitals
look into momentum space
>pic related