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 , we have already investigated , 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.
 K. Nagamine et al., RIKEN Rev. 20, 51 (1999)
 R. H. Scheicher et al., Bull. Am. Phys. Soc., 45, No. 1, 260 (2000)
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