Article
Interactions among residues CD3, E7, E10, and E11 in myoglobins: attempts to simulate the ligand-binding properties of Aplysia myoglobin.
Biochemistry - 11 Jul 1995
Smerdon S J, Krzywda S, Brzozowski A M, Davies G J, Wilkinson A J, Brancaccio A, Cutruzzolá F, Allocatelli C T, Brunori M, Li T
Abstract excerpt
Site-directed mutations have been introduced singly and in combination at residues lysine/arginine45 (CD3), histidine64 (E7), threonine67 (E10), and valine68 (E11) in pig and sperm whale myoglobins. The mutations probe the roles of these key distal pocket residues and represent attempts to mimic the heme environment of Aplysia limacina myoglobin which achieves moderately high O2 affinity in the absence of a...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.