BIO 361 Lecture Notes - Lecture 7: X-Ray Crystallography, Protein Structure, Diffraction
27 Jun 2016
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Biochemistry professor sanford simon stony brook summer 2016. The function of a protein is determined by its tertiary structure. There are three methods for determining the atomic resolution structures of proteins: A very pure protein is required, which is made into a crystal similar to a salt by inducing a slow reduction of solubility of the protein over time. An x-ray beam is then passed through the crystal, which diffracts rays onto a film. Crystal structures are only as accurate as their resolution. High resolution structures are more accurate than low resolution structure (1. 1 angstrom resolution is more accurate than 6. 0 angstrom resolution) Nmr produces ensembles of structures that reveal dynamic areas of tertiary structure. Functional groups have a distinct magnetic shift when associated with different compounds. Peaks that are apart from the diagonal of the noesy are called noes, which give us information about the distance from other chemical groups. Cryoem structures have been determined to 3. 0 angstroms.
