Unfolded proteins and protein folding studied by NMR

Article Abstract:

The use of Nuclear Magnetic Resonance (NMR) is unlimited in the study of chemistry and remains one of the few comprehensive sources for information on unstructured and partly structured proteins and on the protein folding process. NMR solution structure calculations were performed for the micelle-bound peptide hormone glucagon, which is intrinsically unstructured in solution.

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Automated analysis of protein NMR assignments and structures

Article Abstract:

A summary of new methods of automation for determining 3D structures of proteins from Nuclear Magnetic Resonance (NMR), are explained. Manual methods of protein data analysis often involve using laboratory specific, or even user-specific, rules of interpretation and validation.

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NMR studies of modular protein structures and their interactions

Article Abstract:

The biological context of modular proteins is examined. The role of Nuclear Magnetic Resonance in the analysis of the interactions between these modular proteins and their ligands is explained.

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