This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2hhe
From Proteopedia
OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA CHAINS IN HUMAN AND BOVINE HEMOGLOBIN
Template:ABSTRACT PUBMED 7929044
About this Structure
2HHE is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Fronticelli C, Pechik I, Brinigar WS, Kowalczyk J, Gilliland GL. Chloride ion independence of the Bohr effect in a mutant human hemoglobin beta (V1M+H2deleted). J Biol Chem. 1994 Sep 30;269(39):23965-9. PMID:7929044
Page seeded by OCA on Tue Feb 17 00:38:32 2009
