PubMed Health⌕ Search

PubMed · 10739264

The pi-helix translates structure into function.

Abstract

A search for the occurrence of the rare pi-helix was performed with Iditis from the Oxford Molecular Group upon the Protein Data Bank. In 8 of the 10 confirmed crystal structures that harbor the pi-helix, its unique conformation has been linked directly to the formation or stabilization of a specific binding site within the protein. In the discussion to follow, the role for each of these eight pi-helices will be addressed in regard to protein function. It is clear upon closer examination that the conformation of the pi-helix has evolved to provide unique structural features within a variety of proteins.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

T M Weaver. 2000. The pi-helix translates structure into function.. https://doi.org/10.1110/ps.9.1.201

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Nitric oxide photorelease from ruthenium salen complexes in aqueous and organic solutions.

The complexes [Ru(salen)(NO)Cl] and [Ru(salen)(NO)(H(2)O)](+) were shown to release the nitrosyl ligand as nitric oxide upon exposure to visible light in organic and aqueous solutions respectively, by means of UV-visible, EPR, and FTIR spectroscopies. The former was prepared by a new synthetic route and had its structure determined by single-crystal X-ray diffraction. A crystal of the dichloromethane solvate is orthorhombic, space group Fdd2 (No. 43) and formula C(16)H(14)ClN(3)O(3)Ru.CH(2)Cl(2), with Z = 16 and cell parameters a = 25.489(4), b = 33.435(4), and c = 9.3716(9) A. The electronic absorption spectra of the complexes were calculated using the INDO/S method. The water-soluble complex is a potential drug for antitumoral phototreatment.

Crystallography, X-Ray↗