Abstract
Recently published crystallographic data show that functionally important events are frequently accompanied by small, in absolute magnitude, but widespread perturbation of protein structure [l-5]. These conformational rearrangements are still hardly enlightened because they do not usually affect the content of regular structure, the fraction of solvent, exposed aromatic residues or the shape of molecule and therefore could not be detected by optical or hydrodynamic methods. To clarify the physical basis and the functional meaning of such subtle conformational changes it is necessary to know whether they lead to any changes in conformational energy of the protein. To study this we have chosen two derivatives of Hb MetHbHzO and MetHbCN as a model because recently the above-mentioned conformational differences between these two liganded Hbs have been well documented by a sensitive difference Fourier
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