The alpha-helix dipole and the properties of proteins.
Phosphate moieties bind frequently at N-termini of helices in proteins. It is shown that this corresponds with an optimal interaction of the helix dipole and the charged phosphate. This favourable arrangement may have been discovered several times during evolution. In some enzymes, the helix dipole might be used in catalysis.
D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003067:Coenzymes; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010206:Papain; D010710:Phosphates; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013381:Subtilisins; D013884:Thiosulfate Sulfurtransferase
D003067:Coenzymes; D010710:Phosphates; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D013884:Thiosulfate Sulfurtransferase; D013381:Subtilisins; D010206:Papain