Analysis of dynamic properties of a simple globular protein, myoglobin, has demonstrated that it possesses a hier-archically organized energy landscape. It shows two types of specific protein motions, besides vibrations: 1) individual motions of small atomic groups - transitions between conformational substates (CS) of the lower tier 2, and 2) cooperative motions of secondary structure elements (α-helices) - transitions between CS of the upper tier 1. The profile of macromo-lecule dynamic properties is highly heterogeneous. Only vibrations occur near the active center. The number of CS grows towards the periphery where specific type 1 and 2 motions become predominant. Such a picture is consistent with the concept of a protein as 'a random copolymer slightly edited in the vicinity of the active center'.
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