Key result
Multidimensional heteronuclear NMR spectroscopy revealed that the 92 amino acid RNA binding domain of human hnRNP A1 protein exhibits a beta alpha beta beta alpha beta folding pattern.
Population
The first RNA binding domain of the human hnRNP A1 protein (92 amino acids long)
Design
Other
Authors
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hnRNP A1 RBD1 adopts conserved beta alpha beta beta alpha beta fold; extends family homology but leaves functional roles open.
The first RNA binding domain of human hnRNP A1 protein has a beta alpha beta beta alpha beta folding pattern similar to other members of its family.
Garrett et al. (1994) studied this question. Multidimensional heteronuclear NMR spectroscopy was evaluated on Secondary structure and folding topology. Multidimensional heteronuclear NMR spectroscopy revealed that the 92 amino acid RNA binding domain of human hnRNP A1 protein exhibits a beta alpha beta beta alpha beta folding pattern.
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