Recognition and unfolding of human telomeric G-quadruplex by short peptide binding identified from the HRDC domain of BLM helicase

Keyphrases

• Cellular Events 100%
• Short Peptides 100%
• Circular Dichroism 100%
• Peptide Binding 100%
• G-quadruplex 100%
• BLM Helicase 100%
• Human Telomeric G-quadruplex 100%
• Protein-protein Interaction 50%
• Cell Viability 50%
• Stacking Interactions 50%
• Binding Protein 50%
• High Specificity 50%
• Guanine 50%
• Serious Disease 50%
• Biological Effects 50%
• Peptide Complexes 50%
• IC50 Value 50%
• Peptide Concentration 50%
• Secondary Structure 50%
• Peptide Library 50%
• Binding Motif 50%
• Electrophoretic Mobility Shift Assay 50%
• Molecular Docking 50%
• G4 Structure 50%
• G-quadruplex DNA 50%
• Human Telomere 50%
• G-quadruplex Structure 50%
• Hypochromicity 50%
• Parallel G-quadruplex 50%
• Telomeric G-quadruplex 50%

Biochemistry, Genetics and Molecular Biology

• Helicase 100%
• Circular Dichroism 100%
• Protein Interaction 50%
• Solution and Solubility 50%
• Binding Protein 50%
• Cell Viability 50%
• Guanine 50%
• Biological Activity 50%
• Protein Secondary Structure 50%
• Docking (Molecular) 50%
• IC50 50%
• Crystal Structure 50%
• Peptide Library 50%
• Electrophoretic Mobility Shift Assay 50%
• Telomere 50%