Octapeptide simulations, structure

Figure 6. A stereo representation of the "best" minimized structure from the 300K octapeptide simulations.

The MM-EPR approach has been used successfully in a number of recent studies [205,206 328 329]. The most novel is that of the solution structure refinement of a dicopper(II) compound of a cyclic octapeptide[205] which is only the second structure of a dicopper(II) compound of this type of biologically important ligand and the first of a metal compound of an artificial cyclic octapeptide. An important development in this area is a new method for the simulation of EPR spectra (SOPHE)[325,326], which allows the simulation of coupled EPR spectra of polynuclear species with more than two metal centers with any electron spin 0, based on sets of parameters similar to those discussed above. 

B. R. Brooks, in Supercomputer Research in Chemistry and Chemical Engineering, ACS Symposium Series 353. K. F. Jensen, and D. G. Truhlar, Eds., American Chemical Society, Washington, D.C., 1987, pp. 123-145. Applications of Molecular Dynamics for Structural Analysis of Proteins and Peptides. R. H. Reid, C. A. Hooper, and B. R. Brooks, Biopolymers, 28, 525 (1989). Computer Simulations of a Tumor Surface Octapeptide Epitope. 

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