X-ray crystallography of proteins

The successful application of X-ray crystallography of proteins to solution of the structure of lysozyme has been spectacular, but is beyond the scope of this article. However, the enzyme-substrate complexes are of considerable interest, because these substrates and the (structurally similar) inhibitors are carbohydrates. 

SANS on disordered food systems is quite different from X-ray crystallography of protein crystals. The former studies systems in their native solution state, with information limited by various averaging effects. The latter can obtain very detailed information on single proteins in a highly ordered crystal, which is a non-native state. 

One might hope to see evidence in the 3D structure for both the ferric-ferryl conversion and the amino-acid free radical. However, X-ray crystallography of proteins cannot resolve individual hydrogen atoms. Therefore it is important to remember [104] that as the oxidation of cytochrome c peroxidase to compound I involves no change in the number of non-hydrogen atoms, it is possible that... 

J.P. Glusker. 1994. X-ray crystallography of proteins Met/zoife Biochem. Anal. 37 1-72. (PubMed)... 

The a-helix is one of the best-known regular conformational features as a subheading within the secondary structure of polypeptides and is frequently adopted in chains of six or more helicogenic amino acids (see Table 2.1 for a definition of terms and examples). The (3-sheet is another classic conformational structure that has been detected from the earliest days of X-ray crystallography of proteins. Local... 

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