Abstract
Optical spectroscopy provides a wealth of information about protein structure that is difficult to obtain from other methods. Investigations of changes in primary, secondary, tertiary, and quaternary structure are particularly well-suited for optical techniques such as UV absorption, circular dichroism, fluorescence, Raman and infrared spectroscopy, as well as light scattering methods. Each method has unique areas of applicability and contributes to structure determination in a different manner. The application of these methods is demonstrated with examples of studies performed on bovine growth hormone. Some of these include: determination of solution-state structure, monitoring differences between solution- and solid-state structure, determination of molecular size distribution, and investigations of protein folding mechanisms. It is demonstrated that by judicious choice of methods, a reasonably complete description of protein structure can be obtained.
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