Related Experiment Video

Updated: Dec 6, 2025

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
08:07

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

Published on: January 17, 2025

1.9K

Influence of position of hydroxyl group of flavonoids on their binding with single stranded polyriboadenylic acid: A

Susmita Chowdhury1, Sutanwi Bhuiya1, Lucy Haque1

  • 1Biophysical Chemistry Laboratory, Physical Chemistry Section, Department of Chemistry, Jadavpur University, 188 Raja S. C. Mallick Road, Kolkata 700032, India.

Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy
|October 10, 2020
PubMed

Keywords:
ESIPTGroove bindingHypochromismRole of hydroxyl groups

More Related Videos

A Rapid and Quantitative Fluorimetric Method for Protein-Targeting Small Molecule Drug Screening08:34

A Rapid and Quantitative Fluorimetric Method for Protein-Targeting Small Molecule Drug Screening

Published on: October 16, 2015

10.4K
A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates11:49

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates

Published on: August 21, 2018

6.8K

Related Concept Videos

IR and UV–Vis Spectroscopy of Carboxylic Acids01:28

IR and UV–Vis Spectroscopy of Carboxylic Acids

In IR spectroscopy of carboxylic acids, the C=O bond shows a characteristic band between 1710 and 1760 cm⁻¹, and the O–H bond exhibits a broad band between 2500 and 3300 cm⁻¹.
However, the stretching absorptions for the C=O bond vary depending on the structure of carboxylic acids. The C=O bond of the free carboxylic acids shows a higher stretching frequency, 1760 cm−1, while H-bonded carboxylic acids (dimers) exhibit stretching absorptions at a lower frequency,...
5.4K
IR and UV–Vis Spectroscopy of Aldehydes and Ketones01:29

IR and UV–Vis Spectroscopy of Aldehydes and Ketones

Infrared spectroscopy, also known as vibrational spectroscopy, is mainly used to determine the types of bonds and functional groups in molecules. In aldehydes and ketones, the carbonyl (C=O) bond shows an absorption around 1710 cm-1. The C=O bond vibration of an aldehyde occurs at lower frequencies than that of a ketone. In addition to the C=O absorption in an aldehyde, the aldehydic C–H bond also gives two peaks in the 2700–2800 cm-1 range. This absorption, coupled with the...
7.1K
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.
5.9K
Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
486
Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

Factors Affecting Protein-Drug Binding: Protein-Related Factors

Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
415