Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.
Tang, Q
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin. [electronic resource] - Biochemistry May 1998 - 7047-56 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi9729413 doi
Acids
Animals
Guanidine--pharmacology
Heme--chemistry
Histidine--chemistry
Hydrogen-Ion Concentration
Iron--chemistry
Kinetics
Male
Mutagenesis, Site-Directed
Myoglobin--analogs & derivatives
Protein Folding
Spectrophotometry
Spermatozoa
Whales
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin. [electronic resource] - Biochemistry May 1998 - 7047-56 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi9729413 doi
Acids
Animals
Guanidine--pharmacology
Heme--chemistry
Histidine--chemistry
Hydrogen-Ion Concentration
Iron--chemistry
Kinetics
Male
Mutagenesis, Site-Directed
Myoglobin--analogs & derivatives
Protein Folding
Spectrophotometry
Spermatozoa
Whales