Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins

• Published in: PloS one Vol. 5; no. 4; p. e10262
• Main Authors: Malmendal, Anders, Underhaug, Jarl, Otzen, Daniel E, Nielsen, Niels C
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 21.04.2010; Public Library of Science (PLoS)
• Subjects: Animals; Biophysics/Biomacromolecule-Ligand Interactions; Biophysics/Experimental Biophysical Methods; Biophysics/Protein Folding; Cattle; Chemistry; E coli; Escherichia coli; Experiments; Folding; Global Positioning System; Hot Temperature; Hydrogen; Hydrogen atoms; Interdisciplinary aspects; Labeling; Labelling; Lactalbumin; Lactalbumin - chemistry; Ligands; Macromolecules; Magnetic Resonance Spectroscopy - methods; Mapping; Methods; Multivariate analysis; NMR; Nuclear magnetic resonance; Peptide mapping; Pollutants; Principal components analysis; Protein Denaturation; Protein Folding; Proteins; Sodium; Sodium dodecyl sulfate; Sodium lauryl sulfate; Surface active agents; Surfactants; Denmark; Aarhus Denmark
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0010262

To obtain insight into the functions of proteins and their specific roles, it is important to establish efficient procedures for exploring the states that encapsulate their conformational space. Global Protein folding State mapping by multivariate NMR (GPS NMR) is a powerful high-throughput method that provides such an overview. GPS NMR exploits the unique ability of NMR to simultaneously record signals from individual hydrogen atoms in complex macromolecular systems and of multivariate analysis to describe spectral variations from these by a few variables for establishment of, and positioning in, protein-folding state maps. The method is fast, sensitive, and robust, and it works without isotope-labelling. The unique capabilities of GPS NMR to identify different folding states and to compare different unfolding processes are demonstrated by mapping of the equilibrium folding space of bovine alpha-lactalbumin in the presence of the anionic surfactant sodium dodecyl sulfate, SDS, and compare these with other surfactants, acid, denaturants and heat.