Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/80215
Title: Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy
Authors: Gupta, Sebanti
Bhattacharjya, Surajit
Keywords: Nuclear magnetic resonance
Low-energy alternate states
Near-native conformations
Ste11 SAM domain
Issue Date: 2014
Source: Gupta, S., & Bhattacharjya, S. (2014). Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy. Proteins: Structure, Function, and Bioinformatics, 82(11), 2957-2969.
Series/Report no.: Proteins: Structure, Function, and Bioinformatics
Abstract: The sterile alpha motif or SAM domain is one of the most frequently present protein interaction modules with diverse functional attributions. SAM domain of the Ste11 protein of budding yeast plays important roles in mitogen-activated protein kinase cascades. In the current study, urea-induced, at subdenaturing concentrations, structural, and dynamical changes in the Ste11 SAM domain have been investigated by nuclear magnetic resonance spectroscopy. Our study revealed that a number of residues from Helix 1 and Helix 5 of the Ste11 SAM domain display plausible alternate conformational states and largest chemical shift perturbations at low urea concentrations. Amide proton (H/D) exchange experiments indicated that Helix 1, loop, and Helix 5 become more susceptible to solvent exchange with increased concentrations of urea. Notably, Helix 1 and Helix 5 are directly involved in binding interactions of the Ste11 SAM domain. Our data further demonstrate that the existence of alternate conformational states around the regions involved in dimeric interactions in native or near native conditions.
URI: https://hdl.handle.net/10356/80215
http://hdl.handle.net/10220/40455
ISSN: 0887-3585
DOI: 10.1002/prot.24652
Schools: School of Biological Sciences 
Rights: © 2014 Wiley Periodicals, Inc. This is the author created version of a work that has been peer reviewed and accepted for publication by Proteins: Structure, Function, and Bioinformatics, Wiley Periodicals, Inc.. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1002/prot.24652].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

SCOPUSTM   
Citations 50

1
Updated on Jul 20, 2024

Web of ScienceTM
Citations 50

1
Updated on Oct 27, 2023

Page view(s) 50

429
Updated on Jul 23, 2024

Download(s) 20

206
Updated on Jul 23, 2024

Google ScholarTM

Check

Altmetric


Plumx

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.