In order to explore the electron-transfer process in life science, we have been carrying out muSR studies based upon electron labeling mechanisms on a protein, cytochrome c, which is a member of the respiratory chain. In order to deepen the understanding of these muSR data, we intend to determine the muon stopping sites and electronic structure. Our LF muSR data showed a level crossing resonance (LCR) signature for cytochrome c indicated that some portion of muon has a strong energy transfer at specific LF to the surrounding species at the stopping site. The observed LCR data was similar to that of polyglycine (F.Pratt, private communication) and would be attributed to quadruple LCR. In this proposal, we examine LCR of N-methylacetamide, the simplest molecule containing a peptide bond,and glycine–14N (Q=0.16) and–15N (Q = 0)to confirm the stopping sites and possibility of QLCR.