Journal article
Local Structural Preferences and Dynamics Restrictions in the Urea-Denatured State of SUMO-1: NMR Characterization
Abstract
We have investigated by multidimensional NMR the structural and dynamic characteristics of the urea-denatured state of activated SUMO-1, a 97-residue protein belonging to the growing family of ubiquitin-like proteins involved in post-translational modifications. Complete backbone amide and 15N resonance assignments were obtained in the denatured state by using HNN and HN(C)N experiments. These enabled other proton assignments from TOCSY-HSQC …
Authors
Kumar A; Srivastava S; Mishra RK; Mittal R; Hosur RV
Journal
Biophysical Journal, Vol. 90, No. 7, pp. 2498–2509
Publisher
Elsevier
Publication Date
April 2006
DOI
10.1529/biophysj.105.071746
ISSN
0006-3495
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
AmidesAmino Acid SequenceCircular DichroismGlycineHumansHydrogen-Ion ConcentrationLeucineMagnetic Resonance SpectroscopyMolecular Sequence DataProtein ConformationProtein FoldingProtein Processing, Post-TranslationalProtein Structure, SecondaryProtein Structure, TertiaryProtonsSUMO-1 ProteinTemperatureThermodynamicsTime FactorsUrea