1. An Atomistic View on Human Hemoglobin Carbon Monoxide Migration Processes 
M. Fátima Lucas, Víctor Guallar 
Biophysical Journal 
Volume 102, Issue 4, Pages (February 2012)
DOI: /j.bpj
Copyright © 2012 Biophysical Society Terms and Conditions

2. Figure 1
CO digression near a system composed of three residues, the central residue being a phenylalanine. The older version of PELE software was used for the structure on the left, where the corrected versioni was used for the righthand structure.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2012 Biophysical Society Terms and Conditions

3. Figure 2
View of the carbon monoxide exit passages in Mb. The protein is shown in cartoon representation with most of the helices labeled. The ligand, in bead representation, indicates the center of mass of the molecule. Different colors specify the different exit paths, and the pink spheres identify the xenon sites.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2012 Biophysical Society Terms and Conditions

4. Figure 3
Schematic representation of the carbon monoxide exit passages in human Hb. The table contains information concerning the percentage of ligands that exit by each path shown in the figure.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2012 Biophysical Society Terms and Conditions

5. Figure 4
Overall statistics for ligand migration from the active site to the exterior of the protein. Mb and the R and T states for Hb are shown, as are the α-and β-subunits.
Biophysical Journal  , DOI: ( /j.bpj )
Copyright © 2012 Biophysical Society Terms and Conditions