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Abstract
The analysis of peptides and proteins is complicated either by their inherent reactivity (as physical change is produced in peptide structure due to aggregation) or by adsorption of sample material onto container surfaces. The characterization of proteins requires the use of several techniques; each probe measures a particular structural or functional feature. Methods for evaluating the purity and stability of peptides and proteins exist as well as various methods for their structural characterization: size, shape, and conformational changes. These are modifications of secondary and tertiary structures produced in the molecule during preparation, manipulation, and storage.