The alpha-helix dipole and the properties of proteins.

Nature ·Vol. 273 ·No. 5662 ·1978-06-08 ·Pages 443-6

Hol WG, van Duijnen PT, Berendsen HJ

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

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

Chemicals

Coenzymes Phosphates Glyceraldehyde-3-Phosphate Dehydrogenases Thiosulfate Sulfurtransferase Subtilisins Papain

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Hol W G

van Duijnen P T

Berendsen H J

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/273443a0

Published

1978-06-08

Pages

443-6

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/273443a0 View journal details

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The alpha-helix dipole and the properties of proteins.

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