Abstract:
:X-ray crystallographic data to 1.9-A resolution were collected on sperm whale metmyoglobin equilibrated with 7 atm of xenon gas. The results indicate four xenon sites of occupancy from 0.45 to 1.0. These sites are located in interior spaces or packing defects of the myoglobin molecule. The effects of the bound xenon on the protein structure are minor, and we observe a small overall reduction in refined isotropic atomic protein temperature factors. We interpret the results as a confirmation that, on a time-averaged basis, cavities exist within the myoglobin molecule and suggest that the binding of small ligands in these cavities affects the internal motions and conformational substrates of the protein.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Tilton RF Jr,Kuntz ID Jr,Petsko GAdoi
10.1021/bi00308a002subject
Has Abstractpub_date
1984-06-19 00:00:00pages
2849-57issue
13eissn
0006-2960issn
1520-4995journal_volume
23pub_type
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