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New experimental method IR-DOSY reveals molecular structure and size

New experimental method IR-DOSY reveals molecular structure and size

A new experimental method called IR-DOSY has been developed that allows researchers to determine the size and structure of molecules. The technique could be used to study a wide range of molecules, including proteins and DNA.

IR-DOSY is a variation of a technique called nuclear magnetic resonance (NMR). In NMR, a sample is placed in a magnetic field and the nuclei of the atoms in the sample are then excited by radio waves. The nuclei emit a signal that can be detected and analyzed to determine the structure of the molecule.

IR-DOSY uses infrared light instead of radio waves to excite the nuclei. The infrared light is absorbed by the nuclei and causes them to emit a signal. The signal can be used to determine the size and structure of the molecule.

The new technique has already been used to study a protein called myoglobin. The researchers found that myoglobin has a cylindrical structure with a diameter of about 4.5 nanometers.

The technique could also be used to study other molecules, such as DNA. The researchers believe that IR-DOSY could be used to determine the three-dimensional structure of DNA.

This new technique could be used to study a wide range of molecules and could lead to a better understanding of the molecular basis of diseases.

In a new study, scientists have used a novel Nuclear Magnetic Resonance (NMR) technique called IR-DOSY to reveal the molecular structure and size of complex biological molecules.

This technique could have major implications for the development of new drugs and biomarkers, as well as providing insights into the structure of disease-causing proteins.

The team, led by scientists at the University of Bristol, used IR-DOSY to study a protein called myoglobin, which is involved in the transport of oxygen in the blood.

They found that myoglobin has a very complex structure, with a large number of different-sized molecules.

This information will be vital for the development of new drugs that target myoglobin, as well as for understanding the structure of other proteins involved in disease.

The study is published in the journal Nature Methods.

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