A method is described by which bioinformatic concepts and tools can be applied to the study of protein dynamic properties. Sequences are transformed into numerical strings by representing each amino acid by a residue specific average value of the crystallographic alpha carbon B factor. These dynamic sequences are then Fourier transformed. The Fourier coefficients, each of which contains information about the entire sequence, viewed on a specific length scale, can then be used to study a wide variety of dynamic characteristics in a manner which is completely inaccessible using conventional tools.