In vitro selection and analysis of RNA aptamer recognize arginine-rich motif (ARM) model peptide on a QCM.
To study RNA-peptide interactions, we performed an in vitro selection of RNA on a 27 MHz quartz-crystal microbalance (QCM) on which a simple R5 helix peptide was immobilized as a model of N peptide from bacteriophade lambda. The consensus sequences including a GNRA tetraloop were obtained from a random RNA pool after the 7th cycle selection.
Fukusho
S
S
Department of Biomolecular Engineering, Tokyo Institute of Technology, Nagatsuda, Midori-ku, Yokohama, Kanagawa 226-8501, Japan.
Furusawa
H
H
Okahata
Y
Y
D020816:Amino Acid Motifs; D010582:Bacteriophage lambda / Q000235:genetics; D001483:Base Sequence; D001665:Binding Sites; D066298:In Vitro Techniques; D007700:Kinetics; D009690:Nucleic Acid Conformation; D012313:RNA / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D054334:Viral Regulatory and Accessory Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
C059417:N protein, Bacteriophage lambda; D016601:RNA-Binding Proteins; D054334:Viral Regulatory and Accessory Proteins; D012313:RNA