Related Experiment Video
Updated: Jun 6, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Conformational transition of DNA bound to Hfq probed by infrared spectroscopy
Frédéric Geinguenaud1, Vania Calandrini, José Teixeira
1UFR SMBH, Université Paris 13, Bobigny F-93017, France.
Abstract:
Hfq is a bacterial protein involved in RNA metabolism. Besides this, Hfq's role in DNA restructuring has also been suggested. Since this mechanism remains unclear, we examined the DNA conformation upon Hfq binding by combining vibrational spectroscopy and neutron scattering. Our analysis reveals that Hfq, which preferentially interacts with deoxyadenosine rich sequences, induces partial opening of dA-dT sequences accompanied by sugar repuckering of the dA strand and hence results in a heteronomous A/B duplex. Sugar repuckering is probably correlated with a global dehydration of the complex. By taking into account Hfq's preferential binding to A-tracts, which are commonly found in promoters, potential biological implications of Hfq binding to DNA are discussed.
More Related Videos
Related Concept Videos
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)
IR Spectrum Peak Broadening: Hydrogen Bonding
However, the extent of hydrogen bonding influences the observed stretching frequency and band broadening. Intermolecular or intramolecular hydrogen bonding...
IR Frequency Region: Fingerprint Region
The...
IR Frequency Region: X–H Stretching

