| Literature DB >> 661956 |
W G Hol, P T van Duijnen, H J Berendsen.
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.Entities:
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Year: 1978 PMID: 661956 DOI: 10.1038/273443a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962