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

A. Malmendal, J. Underhaug, Daniel E. Otzen, N.C. Nielsen

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

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. textcopyright 2010 Malmendal et al.
OriginalsprogEngelsk
TidsskriftPLOS ONE
Vol/bind5
Udgave nummer4
ISSN1932-6203
DOI
StatusUdgivet - 2010

Citer dette

Malmendal, A. ; Underhaug, J. ; Otzen, Daniel E. ; Nielsen, N.C. / Fast mapping of global protein folding states by multivariate NMR: A GPS for proteins. I: PLOS ONE. 2010 ; Bind 5, Nr. 4.
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Fast mapping of global protein folding states by multivariate NMR: A GPS for proteins. / Malmendal, A.; Underhaug, J.; Otzen, Daniel E.; Nielsen, N.C.

I: PLOS ONE, Bind 5, Nr. 4, 2010.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Fast mapping of global protein folding states by multivariate NMR: A GPS for proteins

AU - Malmendal, A.

AU - Underhaug, J.

AU - Otzen, Daniel E.

AU - Nielsen, N.C.

PY - 2010

Y1 - 2010

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. textcopyright 2010 Malmendal et al.

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. textcopyright 2010 Malmendal et al.

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