First-Principles Theory of µ+ and Mu Trapping in the Protein Chain of Cytochrome c

R. H. Scheicher (SUNY Albany, Albany NY), D. Cammarere (SUNY Albany; Tamarac High School, Brittenkill NY), T. M. Briere (KEK-MSL, Tsukuba, Japan), N. Sahoo (Albany Medical College, Albany NY; SUNY Albany), T. P. Das (SUNY Albany), F. L. Pratt (RIKEN-RAL, Didcot, UK; Clarendon Laboratory, Oxford, UK), K. Nagamine (KEK-MSL; RIKEN, Wako-shi, Japan)

For the interpretation of data on electron transport in proteins from Muon Spin Rotation measurements [1], we have already investigated [2], using the Hartree-Fock Cluster Procedure, the trapping of positive muon (µ+) and muonium (Mu) in a number of single amino-acid molecules and in polyglycine. We are currently applying the method to a part of the protein chain of Cytochrome c, to see which groups there are most attractive for µ+ and Mu, using three nearest neighbor amino-acids on either side of the group under study to simulate the influence of the protein chain, found to be a suitable choice from our investigations on polyglycine. Results for µ+ and Mu trappings will be presented and discussed.

[1] K. Nagamine et al., RIKEN Rev. 20, 51 (1999)
[2] R. H. Scheicher et al., Bull. Am. Phys. Soc., 45, No. 1, 260 (2000)

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