In ONE paragraph, explain 'London Dispersion forces' in proteins?
London Dispersion forces are a type of van der waals force interaction. In proteins they happen between any temporary induced positive and induced negative dipole. Individually they are not strong, but together with thousands or more interactions between amino acids side chains per protein, they hold the protein secondary structure together, and enable the relatively dense packing of proteins. They differ from hydrogen bonds which form on specific, stable dipoles between hydrogen and an electronegative atom like oxygen.