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Biochemistry 1992, 31, 8180-8 190 8180 'H, 13C, and 15 N NMR Backbone Assignments and Secondary Structure of Human -$ Stephan Greek, *? Heinz Nobel, ll Racer Gent, LI Gianni Gotta, ll Alexander M.

How to fill out nmr backbone assignments and

How to fill out nmr backbone assignments and:

1. Start by obtaining the NMR spectra of the protein or molecule you are studying. This can be done either through your own experiments or by accessing existing spectra databases.
2. Carefully analyze the spectra to identify the signals corresponding to the backbone of the molecule. These signals typically arise from the amide protons and carbonyl carbons in proteins.
3. Assign the chemical shifts of these backbone signals by comparing them to published reference values or using computer-assisted prediction tools.
4. Next, determine the connectivity of these backbone signals by analyzing the through-bond and through-space coupling patterns observed in 2D NMR experiments, such as COSY, TOCSY, and NOESY.
5. Use the chemical shifts and connectivity information to establish the sequential order of the amino acid residues in the protein or the order of the monomer units in your molecule.
6. Additionally, it is important to assign the secondary structure elements of the molecule based on the characteristic NMR chemical shifts and coupling patterns associated with secondary structures like alpha-helices and beta-sheets.
7. Verify the backbone assignments by comparing them to other available data, such as crystallography or electron microscopy, if applicable.

Who needs NMR backbone assignments and:

1. Structural biologists and biochemists studying protein structures rely on accurate NMR backbone assignments to determine the folding patterns and dynamic properties of proteins.
2. Drug researchers and medicinal chemists use NMR backbone assignments to study the interactions between small molecules and their protein targets, aiding the design of new drugs.
3. Molecular biologists studying nucleic acids and other biological macromolecules also benefit from NMR backbone assignments to understand their structures and functions.
4. Organic chemists working on the synthesis and characterization of small organic molecules use NMR backbone assignments to confirm the structures and assess the purity of their compounds.
5. Researchers involved in biomolecular engineering and drug discovery projects often use NMR backbone assignments to optimize protein-protein and protein-ligand interactions.

Overall, NMR backbone assignments are crucial for various scientific disciplines involved in understanding the structural and functional aspects of biomolecules.

For pdfFiller’s FAQs

What is nmr backbone assignments?

NMR backbone assignments refer to the process of determining the resonance frequencies of individual atoms in a protein or nucleic acid.

Who is required to file nmr backbone assignments?

Researchers or scientists conducting NMR studies on proteins or nucleic acids are required to file NMR backbone assignments.

How to fill out nmr backbone assignments?

NMR backbone assignments are usually filled out by recording the chemical shifts, coupling constants, and other parameters observed in NMR spectra.

What is the purpose of nmr backbone assignments?

The purpose of NMR backbone assignments is to map out the connectivities between atoms in proteins or nucleic acids, which is crucial for structural determination.

What information must be reported on nmr backbone assignments?

NMR backbone assignments typically include chemical shifts, coupling constants, peak intensities, and spectral parameters for each atom in a protein or nucleic acid.

When is the deadline to file nmr backbone assignments in 2023?

The deadline to file NMR backbone assignments in 2023 is usually dependent on the specific research project or journal submission deadline.

What is the penalty for the late filing of nmr backbone assignments?

The penalty for late filing of NMR backbone assignments can vary, but it may result in delays in publication or rejection from scientific journals.

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