To measure fluorescence and phosphorescence lifetimes of Bence Jones proteins and light chains of immunoglobulins between K77 and K350. Early studies have disclosed a great diversity of fluorescence and phosphorescence spectra associated with the unique sequence protein chains of the light chain of immunoglobulins. Recent advances in nonlinear least squares minimization to optimize model function parameter values for correlated observation pairs offers the technical means to determine protein lifetime parameters. Initial estimates are obtainable through an eigen function expansion. By including the entire second derivatives of parameters of the model and observation, accurate statistical confidence limits for parameters of nonlinear models can be estimated. An attempt to better define groups of proteins of common natural lifetime for tyrosine and tryptophan fluorescence will be made. Temperature dependence can be modeled with a simple Arrhenius activation of a radiation-less process, together with a temperature independent process. Preliminary studies have suggested there is a linear correlation between pre-exponential and exponential parameters - compensation laws. The compensation temperature for the several groups of Bence Jones proteins will be estimated using the general nonlinear least squares procedures.