Abstract
It is only some 50 years ago that biophysicists obtained reliable experimental methods for estimating the molecular weights of biological macromolecules, chiefly as a result of Svedberg's work in developing the ultracentrifuge as an analytical instrument (Svedberg & Pedersen, 1940). Having gained some understanding of the size of proteins, interest soon thereafter turned to the shape and rotational relaxation times of these molecules, and Perrin's work on fluorescence depolarization helped to lay the foundations there (Perrin, 1929). Biophysics had to wait for the development of X-ray spectroscopy of proteins and nucleic acids to provide a picture of the interior structure of biological macromolecules.