Conformational changes in oligo-nucleotides upon binding to a peptide representing the N-terminal region of a viral coat protein. An optical spectroscopy study.
Conformational changes of the oligonucleotides r(A)12, d(GC)5, and d(AT)5 upon binding to a pentacosapeptide representing the RNA-binding N-terminus of the coat protein of cowpea chlorotic mottle virus (CCMV) were studied by using absorption and circular dichroism spectroscopy. The peptide destabilizes the single-stranded structure of r(A)12 at pH 7.2, but disrupts the double-stranded structure of r(A)12 at pH 5.0. However, at pH 4.0, the peptide is not able to disrupt this double-stranded structure. The double-stranded structures of d(GC)5 and d(AT)5 with Watson-Crick base-pairing are stabilized upon binding to the peptide.
Wolfs
C J
CJ
Agricultural University, Department of Molecular Physics, Wageningen, Netherlands.
van der Graaf
M
M
Hemminga
M A
MA
D000227:Adenine Nucleotides / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D001482:Base Composition; D002213:Capsid / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D009838:Oligodeoxyribonucleotides / Q000737:chemistry / Q000378:metabolism; D009841:Oligonucleotides / Q000737:chemistry* / Q000378:metabolism; D009843:Oligoribonucleotides / Q000737:chemistry / Q000378:metabolism; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D010942:Plant Viruses; D011067:Poly dA-dT / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D013816:Thermodynamics
D000227:Adenine Nucleotides; D009838:Oligodeoxyribonucleotides; D009841:Oligonucleotides; D009843:Oligoribonucleotides; D010455:Peptides; C016023:oligo(dA-dT); D011067:Poly dA-dT; C023505:2',5'-oligoadenylate; C052201:oligo(dG-dC)