A simple method to predict protein flexibility using secondary chemical shifts

DOI	Trouver le DOI : https://doi.org/10.1021/ja054842f
Auteur	Rechercher : Berjanskii, Mark V.; Rechercher : Wishart, David S.
Format	Texte, Article
Résumé	Protein motions play a critical role in many biological processes, such as enzyme catalysis, allosteric regulation, antigen-antibody interactions, and protein-DNA binding. NMR spectroscopy occupies a unique place among methods for investigating protein dynamics due to its ability to provide site-specific information about protein motions over a large range of time scales. However, most NMR methods require a detailed knowledge of the 3D structure and/or the collection of additional experimental data (NOEs, T₁, T₂, etc.) to accurately measure protein dynamics. Here we present a simple method based on chemical shift data that allows accurate, quantitative, site-specific mapping of protein backbone mobility without the need of a three-dimensional structure or the collection and analysis of NMR relaxation data. Further, we show that this chemical shift method is able to quantitatively predict per-residue RMSD values (from both MD simulations and NMR structural ensembles) as well as model-free backbone order parameters.
Date de publication	2005-11-02
Dans	JACS: Journals of the American Chemical Society 127, nº 43 (2 novembre 2005) : 14970–14971.
Langue	anglais
Publication du CNRC	Cette publication n’est pas du CNRC Ce sont des publications qui ont été rédigées par un auteur du CNRC, mais avant que celui-ci soit employé du CNRC.
Numéro NPARC	12338298
Exporter la notice	Exporter en format RIS
Signaler une correction	Signaler une correction (s'ouvre dans un nouvel onglet)
Identificateur de l’enregistrement	bd23755d-bbf3-4db9-b0e8-055e79f6d825
Enregistrement créé	2009-09-10
Enregistrement modifié	2020-04-07

Détails de la page

Par :

Conseil national de recherches Canada

Date de modification :: 2026-09-12