Noncovalent probes for the investigation of structure and dynamics of protein-nucleic acid assemblies: The case of NC-mediated dimerization of genomic RNA in HIV-1

Biopolymers

Volumn 91, Issue 4, 2009, Pages 283-296

  Turner, Kevin B ^a   Kohlway, Andrew S ^a   Hagan, Nathan A ^a   Fabris, Daniele ^a  

^a UNIVERSITY OF MARYLAND BALTIMORE COUNTY   (United States)

Author keywords

Aminoglycoside antibiotics; Chaperone activity; Electrospray ionization mass spectrometry; HIV 1 nucleocapsid; Noncovalent probes; Nucleic acid ligands; RNA dimerization and isomerization

Indexed keywords

AMINOGLYCOSIDE ANTIBIOTICS; CHAPERONE ACTIVITY; ELECTROSPRAY IONIZATION MASS SPECTROMETRY; HIV-1 NUCLEOCAPSID; NONCOVALENT PROBES; NONCOVALENT; NUCLEOCAPSIDS;

ANTIBIOTICS; BINDERS; BINDING ENERGY; BINDING SITES; BIOMOLECULES; DIMERIZATION; ELECTRON TRANSITIONS; ELECTROSPRAY IONIZATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROPHOBICITY; IONIZATION; ISOMERIZATION; ISOMERS; LIGANDS; MASS SPECTROMETERS; MASS SPECTROMETRY; POLYMERS; PROBES; RNA; SPECTRUM ANALYSIS; GENES; LINGUISTICS; PARTICLE DETECTORS; PROTEINS; VIRUSES;

NUCLEIC ACIDS;

AMINOGLYCOSIDE ANTIBIOTIC AGENT; DISTAMYCIN A; FRAMYCETIN; GAG PROTEIN; GENOMIC RNA; KANAMYCIN A; KANAMYCIN B; MITOXANTRONE; NUCLEOCAPSID PROTEIN; PAROMOMYCIN; PEPTIDE NUCLEIC ACID; TOBRAMYCIN; DIMER; POLYCATION; RIBONUCLEOPROTEIN;

ARTICLE; BINDING SITE; CONTROLLED STUDY; DIMERIZATION; ELECTROSPRAY MASS SPECTROMETRY; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROGEN BOND; HYDROPHOBICITY; INTERCALATION COMPLEX; ISOMERIZATION; NONHUMAN; PROTEIN RNA BINDING; VIRUS GENOME; BINDING AFFINITY; IN VITRO STUDY; KISSING LOOP DIMER; LIGAND BINDING; MOLECULAR DYNAMICS; NUCLEOTIDE BINDING SITE; RNA ANALYSIS; RNA PROBE; RNA STRUCTURE; STEM LOOP 1; STRUCTURE ANALYSIS; VIRUS NUCLEOCAPSID;

DIMERIZATION; GENOME, VIRAL; HIV-1; LIGANDS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR PROBES; MOLECULAR STRUCTURE; NUCLEOCAPSID; NUCLEOCAPSID PROTEINS; RNA, VIRAL;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 65249190323     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21107     Document Type: Article

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