biostudies-literatureDeKoster GTNCRR NIH HHSNIGMS NIH HHS208-19https://www.ebi.ac.uk/biostudies/studies/S-EPMC4119282biostudies-literatureUnknown107(1)The U1A/U2B″/SNF family of small nuclear ribonucleoproteins uses a phylogenetically conserved RNA recognition motif (RRM1) to bind RNA stemloops in U1 and/or U2 small nuclear RNA (snRNA). RRMs are characterized by their α/β sandwich topology, and these RRMs use their β-sheet as the RNA binding surface. Unique to this RRM family is the tyrosine-glutamine-phenylalanine (YQF) triad of solvent-exposed residues that are displayed on the β-sheet surface; the aromatic residues form a platform for RNA nucleobases to stack. U1A, U2B″, and SNF have very different patterns of RNA binding affinity and specificity, however, so here we ask how YQF in Drosophila SNF RRM1 contributes to RNA binding, as well as to domain stability and dynamics. Thermodynamic double-mutant cycles using tyrosine and phenylalBiophysical journalA compare-and-contrast NMR dynamics study of two related RRMs: U1A and SNF.PMC4119282R01 GM0964441R01 GM096444P41 RR002301P41GM10399P41RR02301DeKoster GTHall KBDelaney KJfalseA compare-and-contrast NMR dynamics study of two related RRMs: U1A and SNF.The U1A/U2B″/SNF family of small nuclear ribonucleoproteins uses a phylogenetically conserved RNA recognition motif (RRM1) to bind RNA stemloops in U1 and/or U2 small nuclear RNA (snRNA). RRMs are characterized by their α/β sandwich topology, and these RRMs use their β-sheet as the RNA binding surface. Unique to this RRM family is the tyrosine-glutamine-phenylalanine (YQF) triad of solvent-exposed residues that are displayed on the β-sheet surface; the aromatic residues form a platform for RNA nucleobases to stack. U1A, U2B″, and SNF have very different patterns of RNA binding affinity and specificity, however, so here we ask how YQF in Drosophila SNF RRM1 contributes to RNA binding, as well as to domain stability and dynamics. Thermodynamic double-mutant cycles using tyrosine and phenylal2014-01-01T00:00:00Z2014 Jul2026-04-30T01:09:04.874Z2026-04-07T15:42:58.526ZS-EPMC41192822498835510.1016/j.bpj.2014.05.026