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Oxygen migration pathways in NO-bound truncated hemoglobin
Pierre André Cazade
, Markus Meuwly
University of Basel
Research output
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peer-review
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Chemistry
Nitric Oxide
100%
Atomistic Simulation
66%
Dioxygen
66%
Heme
66%
Free Energy
66%
Energy Barrier
33%
Phenylalanine Residue
33%
Biochemistry, Genetics and Molecular Biology
Nitric Oxide
100%
Dynamics
66%
Mycobacterium Tuberculosis
66%
Active Site
33%
Probability Distribution
33%
Phenylalanine
33%
Pharmacology, Toxicology and Pharmaceutical Science
Truncated Hemoglobin
100%
Nitric Oxide
75%
Heme
50%
Mycobacterium Tuberculosis
50%
Phenylalanine
25%
Iron
25%
Immunology and Microbiology
Hemoglobin
100%
Dynamics
50%
Mycobacterium Tuberculosis
50%
Heme
50%
Phenylalanine
25%