Abstract
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.
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Catalysis
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Chemical Phenomena
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Chemistry, Physical
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Coenzymes
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Glyceraldehyde-3-Phosphate Dehydrogenases
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Papain
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Phosphates*
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Protein Conformation*
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Structure-Activity Relationship
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Subtilisins
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Thiosulfate Sulfurtransferase
Substances
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Coenzymes
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Phosphates
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Glyceraldehyde-3-Phosphate Dehydrogenases
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Thiosulfate Sulfurtransferase
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Subtilisins
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Papain