Early progress reported in designing drugs that target 'disordered' proteins - Phys.Org
Early progress reported in designing drugs that target 'disordered' proteins - Phys.Org
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Early progress reported in designing drugs that target 'disordered' proteins
Phys.Org
The p27 protein works by binding to an enzyme and forming a complex that blocks cell division. This type of regulation is necessary to keep cells in check when not otherwise instructed to divide. In this study St. Jude researchers used NMR...
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12-01-2015 11:22 PM
A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins
A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins
Abstract
Sequence specific resonance assignment is the prerequisite for the NMR-based analysis of the conformational ensembles and their underlying dynamics of intrinsically disordered proteins. However, rapid solvent exchange in intrinsically disordered proteins often complicates assignment strategies based on HN-detection. Here we present a six-dimensional alpha proton detection-based automated projection spectroscopy (APSY)...
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11-04-2014 01:02 AM
[NMR paper] Novel methods based on 13C detection to study intrinsically disordered proteins
Novel methods based on 13C detection to study intrinsically disordered proteins
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): Isabella C. Felli , Roberta Pierattelli</br>
Intrinsically disordered proteins (IDPs) are characterized by highly flexible solvent exposed backbones and can sample many different conformations. These properties confer them functional advantages, complementary to those of folded proteins, which need to be characterized to expand our view of how protein structural and dynamic features affect...
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03-22-2014 01:28 AM
[NMR paper] NMR based solvent exchange experiments to understand the conformational preference of intrinsically disordered proteins using FG-nucleoporin peptide as a model.
NMR based solvent exchange experiments to understand the conformational preference of intrinsically disordered proteins using FG-nucleoporin peptide as a model.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles NMR based solvent exchange experiments to understand the conformational preference of intrinsically disordered proteins using FG-nucleoporin peptide as a model.
Biopolymers. 2013 Sep 4;
Authors: Heisel KA, Krishnan VV
...
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09-17-2013 11:36 PM
An assignment of intrinsically disordered regions of proteins based on NMR structures
An assignment of intrinsically disordered regions of proteins based on NMR structures
January 2013
Publication year: 2013
Source:Journal of Structural Biology, Volume 181, Issue 1</br>
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Intrinsically disordered proteins (IDPs) do not adopt stable three-dimensional structures in physiological conditions, yet these proteins play crucial roles in biological phenomena. In most cases, intrinsic disorder manifests itself in segments or domains of an IDP, called intrinsically disordered regions (IDRs), but fully disordered IDPs also exist. Although IDRs can be detected as...
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02-03-2013 10:13 AM
Extension of the HA-detection based approach: (HCA)CON(CA)H and (HCA)NCO(CA)H experiments for the main-chain assignment of intrinsically disordered proteins
Extension of the HA-detection based approach: (HCA)CON(CA)H and (HCA)NCO(CA)H experiments for the main-chain assignment of intrinsically disordered proteins
Abstract Extensive resonance overlap exacerbates assignment of intrinsically disordered proteins (IDPs). This issue can be circumvented by utilizing 15N, 13C� and 1HN spins, where the chemical shift dispersion is mainly dictated by the characteristics of consecutive amino acid residues. Especially 15N and 13C� spins offer superior chemical shift dispersion in comparison to 13Cα and 13Cβ spins. However, HN-detected experiments...