[NMR paper] Cost-effective large-scale expression of proteins for NMR studies.
Cost-effective large-scale expression of proteins for NMR studies.
Related Articles Cost-effective large-scale expression of proteins for NMR studies.
J Biomol NMR. 2018 May 19;:
Authors: Klopp J, Winterhalter A, Gébleux R, Scherer-Becker D, Ostermeier C, Gossert AD
Abstract
We present protocols for high-level expression of isotope-labelled proteins in E. coli in cost-effective ways. This includes production of large amounts of unlabeled proteins and 13C-methyl methionine labeling in rich media, where yields of up to a gram of...
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05-21-2018 06:16 PM
Cost-effective large-scale expression of proteins for NMR studies
Cost-effective large-scale expression of proteins for NMR studies
Abstract
We present protocols for high-level expression of isotope-labelled proteins in E. coli in cost-effective ways. This includes production of large amounts of unlabeled proteins and 13C-methyl methionine labeling in rich media, where yields of up to a gram of soluble protein per liter of culture are reached. Procedures for uniform isotope labeling of 2H, 13C and 15N using auto-induction or isopropyl-β-d-1-thiogalactopyranoside-induction are described, with primary focus on...
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05-19-2018 05:41 PM
[NMR paper] NMR studies of large proteins.
NMR studies of large proteins.
Related Articles NMR studies of large proteins.
J Mol Biol. 2017 Jul 17;:
Authors: Jiang Y, Kalodimos CG
Abstract
Recent breakthroughs in isotope-labeling and pulse sequence techniques have enabled the Nuclear Magnetic Resonance (NMR) characterization of large protein systems with molecular weights of hundreds of kDa. NMR studies of a great variety of large proteins have provided unique insights into the binding, dynamic, and allosteric mechanisms. Here we present a brief summary of these...
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07-22-2017 09:28 PM
NMR studies of large proteins
NMR studies of large proteins
Publication date: Available online 17 July 2017
Source:Journal of Molecular Biology</br>
Author(s): Yajun Jiang, Charalampos G. Kalodimos</br>
Recent breakthroughs in isotope-labeling and pulse sequence techniques have enabled the Nuclear Magnetic Resonance (NMR) characterization of large protein systems with molecular weights of hundreds of kDa. NMR studies of a great variety of large proteins have provided unique insights into the binding, dynamic, and allosteric mechanisms. Here we present a brief summary of these developments by...
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07-18-2017 07:52 AM
NMR methods for structural studies of large monomeric and multimeric proteins
NMR methods for structural studies of large monomeric and multimeric proteins
Publication date: Available online 11 July 2013
Source:Current Opinion in Structural Biology</br>
Author(s): Dominique P Frueh , Andrew C Goodrich , Subrata H Mishra , Scott R Nichols</br>
NMR structural studies of large monomeric and multimeric proteins face distinct challenges. In large monomeric proteins, the common occurrence of frequency degeneracies between residues impedes unambiguous assignment of NMR signals. To overcome this barrier, nonuniform sampling (NUS) is used to...
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07-12-2013 04:06 AM
[NMR paper] Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N a
Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.
J Mol Biol. 1996 Dec 20;264(5):1101-16
Authors: Venters RA, Farmer BT, Fierke CA, Spicer LD
Perdeuteration of all non-exchangeable proton sites can...
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