Related ArticlesUnambiguous Assignment of Short- and Long-Range Structural Restraints by Solid-State NMR Spectroscopy with Segmental Isotope Labeling.
Chembiochem. 2014 Nov 12;
Authors: Schubeis T, Lührs T, Ritter C
Abstract
We present an efficient method for the reduction of spectral complexity in the solid-state NMR spectra of insoluble protein assemblies, without loss of signal intensity. The approach is based on segmental isotope labeling by using the split intein DnaE from Nostoc punctiforme. We show that the segmentally (13) C,(15) N-labeled prion domain of HET-s exhibits significantly reduced spectral overlap while retaining the wild-type structure and spectral quality. A large number of unambiguous distance restraints were thus collected from a single two-dimensional (13) C,(13) C cross-correlation spectrum. The observed resonances could be unambiguously identified as intramolecular without the need for preparing a dilute, less sensitive sample.
PMID: 25394265 [PubMed - as supplied by publisher]
[NMR paper] Non-covalent spin labeling of riboswitch RNAs to obtain long-range structural NMR restraints.
Non-covalent spin labeling of riboswitch RNAs to obtain long-range structural NMR restraints.
Related Articles Non-covalent spin labeling of riboswitch RNAs to obtain long-range structural NMR restraints.
ACS Chem Biol. 2014 Mar 27;
Authors: Helmling C, Bessi I, Wacker A, Schnorr KA, Jonker HR, Richter C, Wagner D, Kreibich M, Schwalbe H
Abstract
Paramagnetic relaxation enhancement (PRE) NMR is a powerful method to study structure, dynamics and function of proteins. Up to now, the application of PRE NMR on RNAs is a significant challenge...
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03-29-2014 01:00 PM
[NMR paper] Sparse labeling of proteins: Structural characterization from long range constraints
Sparse labeling of proteins: Structural characterization from long range constraints
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): James H. Prestegard , David A. Agard , Kelley W. Moremen , Laura A. Lavery , Laura C. Morris , Kari Pederson</br>
Structural characterization of biologically important proteins faces many challenges associated with degradation of resolution as molecular size increases and loss of resolution improving tools such as perdeuteration when non-bacterial hosts must be used for expression. In...
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03-22-2014 01:28 AM
[NMR paper] Amino Acid-Selective Segmental Isotope Labeling of Multidomain Proteins for Structural Biology.
Amino Acid-Selective Segmental Isotope Labeling of Multidomain Proteins for Structural Biology.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Amino Acid-Selective Segmental Isotope Labeling of Multidomain Proteins for Structural Biology.
Chembiochem. 2013 Jan 30;
Authors: Michel E, Skrisovska L, Wüthrich K, Allain FH
Abstract
Current solution NMR techniques enable structural investigations of proteins in molecular particles with sizes...
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02-03-2013 10:19 AM
Segmental isotope labeling of proteins for NMR structural study using a protein S tag for higher expression and solubility
Segmental isotope labeling of proteins for NMR structural study using a protein S tag for higher expression and solubility
Abstract A common obstacle to NMR studies of proteins is sample preparation. In many cases, proteins targeted for NMR studies are poorly expressed and/or expressed in insoluble forms. Here, we describe a novel approach to overcome these problems. In the protein S tag-intein (PSTI) technology, two tandem 92-residue N-terminal domains of protein S (PrS2) from Myxococcus xanthus is fused at the N-terminal end of a protein to enhance its expression and solubility. Using...
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03-08-2012 08:46 AM
A segmental labeling strategy for unambiguous determination of domainâ??domain interactions of large multi-domain proteins
A segmental labeling strategy for unambiguous determination of domainâ??domain interactions of large multi-domain proteins
Abstract NMR structural determination of large multi-domain proteins is a challenging task due to significant spectral overlap with a particular difficulty in unambiguous identification of domainâ??domain interactions. Segmental labeling is a NMR strategy that allows for isotopically labeling one domain and leaves the other domain unlabeled. This significantly simplifies spectral overlaps and allows for quick identification of domainâ??domain interaction. Here, a...
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07-08-2011 07:01 PM
NMR order parameters calculated in an expanding reference frame: identifying sites of short- and long-range motion
NMR order parameters calculated in an expanding reference frame: identifying sites of short- and long-range motion
Abstract NMR order parameters are calculated from molecular dynamics computer simulations of ubiquitin and the apo (Ca2+-free) state of calbindin D9k. Calculations are performed in an expanding reference frame so as to discriminate between the effects of short- and long-range motions. This approach reveals that the dominant contributions to the order parameters are short-range. Longer-range contributions are limited to specific sites, many of which have been recognized in...
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04-24-2011 03:40 AM
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
J Am Chem Soc. 2011 Mar 24;
Authors: Linser R, Bardiaux B, Higman V, Fink U, Reif B
Magic-angle spinning (MAS) solid-state NMR becomes an increasingly important tool for the determination of structures of membrane...
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03-26-2011 07:00 PM
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
Rasmus Linser, Benjamin Bardiaux, Victoria Higman, Uwe Fink and Bernd Reif
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja110222h/aop/images/medium/ja-2010-10222h_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja110222h
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Dh0EBf8PwcY
Unambiguous Assignment of Short- and Long-Range Structural Restraints by Solid-State NMR Spectroscopy with Segmental Isotope Labeling.
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