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Article

Short hydrogen bonds in photoactive yellow protein.

Acta crystallographica. Section D, Biological crystallography - 1 Jun 2004

Anderson Spencer, Crosson Sean, Moffat Keith

Abstract excerpt

Eight high-resolution crystal structures of the ground state of photoactive yellow protein (PYP) solved under a variety of conditions reveal that its chromophore is stabilized by two unusually short hydrogen bonds. Both Tyr42 Oeta and Glu46 Oepsilon are separated from the chromophore phenolate oxygen by less than the sum of their atomic van der Waals radii, 2.6 angstroms. This is characteristic of strong hydrogen...

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Source

Identifiers

PMID: 15159559
DOI: 10.1107/S090744490400616X

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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