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. Author manuscript; available in PMC: 2013 Mar 15.
Published in final edited form as: J Phys Chem B. 2012 Mar 6;116(10):3397–3410. doi: 10.1021/jp212148x

Figure 1.

Figure 1

(a) Myoglobin in ribbon representation, with the indication of the four xenon cavities (transparent orange spheres). Elements of secondary structure (helices E, F, G, H and loops CD and FG) are also indicated. (b) The heme pocket with the relevant residues lining the binding site (above the heme plane) and the proximal histidine (below the heme plane); the isopropionate side chains are also indicated. From left to right: native, V68W and L29F mutants (structures as in 1MBC.pdb, 20H9.pdb and 2G0R.pdb). Images were prepared with the VMD program.48