Planar Stacking Interactions of Arginine and Aromatic Side-Chains in Proteins
β Scribed by Maria M. Flocco; Sherry L. Mowbray
- Book ID
- 115626403
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 570 KB
- Volume
- 235
- Category
- Article
- ISSN
- 0022-2836
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Several studies have analysed aromatic interactions, involving mostly phenylalanine, tyrosine and tryptophan. Only a few studies have considered histidine as an interacting aromatic residue. An extensive analysis of aromatic His-X interactions is performed here on a data set of 593 PDB structures: 6
The study of the tryptophanαhistidine adducts, derived from the crystal Ε½ . structures available in the Brookhaven Protein Data Bank PDB , using as model systems Ε½ . w
Although relatively rare, the tryptophan residue (Trp), with its large hydrophobic surface, has a unique role in the folded structure and the binding site of many proteins, and its fluorescence properties make it very useful in studying the structures and dynamics of protein molecules in solution. A