Determination of the secondary structure and folding topology of an RNA binding domain of mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy

Multidimensional heteronuclear nuclear magnetic resonance spectroscopy yields the folding topology and secondary structure of the first RNA binding domain of the hnRNP A1 protein. A beta-alpha-beta-beta-alpha-beta folding pattern is exhibited by amino acid long chains, which are arranged in four-stranded antiparallel beta-sheet supported by two alpha-helices. The loops which attach the secondary structural elements transform the binding proteins of the structurally-classified RNA.