1ajh
From Proteopedia
PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K
Overview
Myoglobin's reversible binding of oxygen is a model for studies of protein control of ligand binding and discrimination. Protein relaxation and geminate ligand rebinding subsequent to ligand photodissociation have been studied extensively by a variety of techniques. The ps to ns time scales for these processes are still much shorter than the ms time resolution of X-ray diffraction experiments, but it may be possible to trap these intermediates at low temperatures. We report here an X-ray diffraction investigation of structural changes induced by photolysis of carbonmonoxy myoglobin crystals at 40 K. Our results provide a structural basis for the interpretation of ambient and low temperature spectroscopic observations and molecular dynamics simulations of the ligand photodissociation and binding processes in haem proteins.
About this Structure
1AJH is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
Reference
Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K., Teng TY, Srajer V, Moffat K, Nat Struct Biol. 1994 Oct;1(10):701-5. PMID:7634074 Page seeded by OCA on Fri May 2 10:21:03 2008
