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

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 t...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Anders Malmendal, Jarl Underhaug, Daniel E Otzen, Niels C Nielsen
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/808ac2ba660e45cb8bce49edc17021c7
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:808ac2ba660e45cb8bce49edc17021c7
record_format	dspace
spelling	oai:doaj.org-article:808ac2ba660e45cb8bce49edc17021c72021-11-25T06:24:26ZFast mapping of global protein folding states by multivariate NMR: a GPS for proteins.1932-620310.1371/journal.pone.0010262https://doaj.org/article/808ac2ba660e45cb8bce49edc17021c72010-04-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20421996/?tool=EBIhttps://doaj.org/toc/1932-6203To 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.Anders MalmendalJarl UnderhaugDaniel E OtzenNiels C NielsenPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 4, p e10262 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anders Malmendal Jarl Underhaug Daniel E Otzen Niels C Nielsen Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins.
description	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.
format	article
author	Anders Malmendal Jarl Underhaug Daniel E Otzen Niels C Nielsen
author_facet	Anders Malmendal Jarl Underhaug Daniel E Otzen Niels C Nielsen
author_sort	Anders Malmendal
title	Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins.
title_short	Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins.
title_full	Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins.
title_fullStr	Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins.
title_full_unstemmed	Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins.
title_sort	fast mapping of global protein folding states by multivariate nmr: a gps for proteins.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/808ac2ba660e45cb8bce49edc17021c7
work_keys_str_mv	AT andersmalmendal fastmappingofglobalproteinfoldingstatesbymultivariatenmragpsforproteins AT jarlunderhaug fastmappingofglobalproteinfoldingstatesbymultivariatenmragpsforproteins AT danieleotzen fastmappingofglobalproteinfoldingstatesbymultivariatenmragpsforproteins AT nielscnielsen fastmappingofglobalproteinfoldingstatesbymultivariatenmragpsforproteins
_version_	1718413753811206144

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

Ejemplares similares