Can NMR be used for proteins?

NMR spectroscopy is the only method that allows the determination of three-dimensional structures of proteins molecules in the solution phase. NMR spectroscopy can be applied to structure determination by routine NMR techniques for proteins in the size range between 5 and 25 kDa.

How is protein structure studied?

The most common method used to study protein structures is X-ray crystallography. With this method, solid crystals of purified protein are placed in an X-ray beam, and the pattern of deflected X rays is used to predict the positions of the thousands of atoms within the protein crystal.

What can NMR determine?

For example, NMR can quantitatively analyze mixtures containing known compounds. Once the basic structure is known, NMR can be used to determine molecular conformation in solution as well as studying physical properties at the molecular level such as conformational exchange, phase changes, solubility, and diffusion.

How much protein do you need for NMR?

Structure determination by NMR typically requires a protein concentration of 0.5 mM or greater, stable for several days at the desired temperature, usually 20-40oC. Proteins and peptides should be dissolved in a suitable buffer (10-50 mM) with 10\% D2O.

What is NMR and how does it work?

How Does NMR Actually Work? When molecules are placed in a strong magnetic field, the nuclei of some atoms will begin to behave like small magnets. The resonant frequencies of the nuclei are then measured and converted into an NMR spectrum that displays all of the right frequencies as peaks on a graph.

How does an NMR experiment work?

How is NMR used in the food industry?

NMR techniques are used successfully in various food systems for quality control and research. NMR spectroscopy is used to determine structure of proteins, aminoacid profile, carotenoids, organic acids, lipid fractions, the mobility of the water in foods.

How do you make a protein sample for NMR?