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

TY - JOUR

T1 - Fast mapping of global protein folding states by multivariate NMR:

T2 - a GPS for proteins

AU - Malmendal, Anders

AU - Underhaug, Jarl

AU - Otzen, Daniel

AU - Nielsen, Niels Chr

PY - 2010/4/21

Y1 - 2010/4/21

N2 - 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 a-lactalbumin in the presence of the anionic surfactant sodium dodecyl sulfate, SDS, and compare these with other surfactants, acid, denaturants and heat.

AB - 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 a-lactalbumin in the presence of the anionic surfactant sodium dodecyl sulfate, SDS, and compare these with other surfactants, acid, denaturants and heat.

U2 - 10.1371/journal.pone.0010262

DO - 10.1371/journal.pone.0010262

M3 - Journal article

C2 - 20421996

SN - 1932-6203

VL - 5

SP - e10262

JO - PLoS Computational Biology

JF - PLoS Computational Biology

IS - 4

ER -