Unique motifs and hydrophobic interactions shape the binding of modified DNA ligands to protein targets.
Davies, Douglas R
Unique motifs and hydrophobic interactions shape the binding of modified DNA ligands to protein targets. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America Dec 2012 - 19971-6 p. digital
Publication Type: Journal Article
1091-6490
10.1073/pnas.1213933109 doi
Amino Acid Motifs--genetics
Aptamers, Nucleotide--chemistry
Becaplermin
Crystallography, X-Ray
DNA Primers--genetics
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Molecular Sequence Data
Molecular Structure
Phosphorylation
Protein Binding
Proto-Oncogene Proteins c-sis--chemistry
SELEX Aptamer Technique--methods
Sequence Analysis, DNA
Transition Temperature
Unique motifs and hydrophobic interactions shape the binding of modified DNA ligands to protein targets. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America Dec 2012 - 19971-6 p. digital
Publication Type: Journal Article
1091-6490
10.1073/pnas.1213933109 doi
Amino Acid Motifs--genetics
Aptamers, Nucleotide--chemistry
Becaplermin
Crystallography, X-Ray
DNA Primers--genetics
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Molecular Sequence Data
Molecular Structure
Phosphorylation
Protein Binding
Proto-Oncogene Proteins c-sis--chemistry
SELEX Aptamer Technique--methods
Sequence Analysis, DNA
Transition Temperature