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Daniel Otzen

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

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Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins. / Malmendal, Anders; Underhaug, Jarl; Otzen, Daniel E; Nielsen, Niels Christian.

In: P L o S One, Vol. 5, No. 4, 21.04.2010, p. e10262.

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Malmendal, Anders ; Underhaug, Jarl ; Otzen, Daniel E ; Nielsen, Niels Christian. / Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins. In: P L o S One. 2010 ; Vol. 5, No. 4. pp. e10262.

Bibtex

@article{e103cbcf6cbb43b9baca21b1693e03f2,
title = "Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins",
abstract = "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.",
author = "Anders Malmendal and Jarl Underhaug and Otzen, {Daniel E} and Nielsen, {Niels Christian}",
year = "2010",
month = apr,
day = "21",
doi = "10.1371/journal.pone.0010262",
language = "English",
volume = "5",
pages = "e10262",
journal = "P L o S One",
issn = "1932-6203",
publisher = "public library of science",
number = "4",

}

RIS

TY - JOUR

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

AU - Malmendal, Anders

AU - Underhaug, Jarl

AU - Otzen, Daniel E

AU - Nielsen, Niels Christian

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 alpha-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 alpha-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

VL - 5

SP - e10262

JO - P L o S One

JF - P L o S One

SN - 1932-6203

IS - 4

ER -