Related ArticlesNMR Structure Determinations of Small Proteins Using only One Fractionally 20% 13C- and Uniformly 100% 15N-Labeled Sample.
Molecules. 2021 Feb 01;26(3):
Authors: Heikkinen HA, Backlund SM, Iwaï H
Abstract
Uniformly 13C- and 15N-labeled samples ensure fast and reliable nuclear magnetic resonance (NMR) assignments of proteins and are commonly used for structure elucidation by NMR. However, the preparation of uniformly labeled samples is a labor-intensive and expensive step. Reducing the portion of 13C-labeled glucose by a factor of five using a fractional 20% 13C- and 100% 15N-labeling scheme could lower the total chemical costs, yet retaining sufficient structural information of uniformly [13C, 15N]-labeled sample as a result of the improved sensitivity of NMR instruments. Moreover, fractional 13C-labeling can facilitate reliable resonance assignments of sidechains because of the biosynthetic pathways of each amino-acid. Preparation of only one [20% 13C, 100% 15N]-labeled sample for small proteins (
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[NMR paper] On the problem of resonance assignments in solid state NMR of uniformly (15)N,(13)C-labeled proteins.
On the problem of resonance assignments in solid state NMR of uniformly (15)N,(13)C-labeled proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif On the problem of resonance assignments in solid state NMR of uniformly (15)N,(13)C-labeled proteins.
J Magn Reson. 2015 Apr;253:166-72
Authors: Tycko R
Abstract
Determination of accurate resonance assignments from multidimensional chemical shift correlation spectra is one of the major problems in...
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03-24-2015 09:58 PM
On the problem of resonance assignments in solid state NMR of uniformly 15N,13C-labeled proteins
On the problem of resonance assignments in solid state NMR of uniformly 15N,13C-labeled proteins
Publication date: April 2015
Source:Journal of Magnetic Resonance, Volume 253</br>
Author(s): Robert Tycko</br>
Determination of accurate resonance assignments from multidimensional chemical shift correlation spectra is one of the major problems in biomolecular solid state NMR, particularly for relative large proteins with less-than-ideal NMR linewidths. This article investigates the difficulty of resonance assignment, using a computational Monte Carlo/simulated...
13 C α CEST experiment on uniformly 13 C-labeled proteins
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Abstract
A new HSQC-based 13Cα CEST pulse scheme is proposed, which is suitable for uniformly 13C- or 13C, 15N-labeled samples in either water or heavy water. Except for Thr and Ser residues, the sensitivity of this scheme for uniformly labeled samples is similar to that of the previous scheme for selectively 13Cα-labeled samples with 100Â*% isotope enrichment. The experiment is demonstrated on an acyl carrier protein domain. Our 13Cα CEST data reveal that the minor state of the acyl...
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12-03-2014 04:05 PM
NMR structure analysis of uniformly 13C-labeled carbohydrates
NMR structure analysis of uniformly 13C-labeled carbohydrates
Abstract
In this study, a set of nuclear magnetic resonance experiments, some of them commonly used in the study of 13C-labeled proteins and/or nucleic acids, is applied for the structure determination of uniformly 13C-enriched carbohydrates. Two model substances were employed: one compound of low molecular weight and one compound of medium molecular weight (13C-enriched O-antigenic polysaccharide isolated from Escherichia coli O142, ~10Â*kDa). The first step in this approach involves...
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[NMR paper] NMR structure analysis of uniformly (13)C-labeled carbohydrates.
NMR structure analysis of uniformly (13)C-labeled carbohydrates.
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J Biomol NMR. 2014 Apr 26;
Authors: Fontana C, Kovacs H, Widmalm G
Abstract
In this study, a set of nuclear magnetic resonance experiments, some of them commonly used in the study of (13)C-labeled proteins and/or nucleic acids, is applied for the structure determination of uniformly (13)C-enriched carbohydrates. Two model substances were employed: one compound of low molecular weight ...
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Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements
Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements
Publication date: Available online 21 March 2014
Source:Protein Expression and Purification</br>
Author(s): Tomáš Kroupa , Jan Prchal , Michal Doležal , Tomáš Ruml , Richard Hrabal</br>
Nuclear magnetic resonance (NMR) is a powerful technique for solving protein structures orstudying their interactions. However, it requires molecules labeled with NMR sensitive isotopes like carbon13C and nitrogen15N. The recombinant expression of labeled proteins is simple...
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03-22-2014 01:28 AM
[NMR paper] Selective 'unlabeling' of amino acids in fractionally 13C labeled proteins: an approa
Selective 'unlabeling' of amino acids in fractionally 13C labeled proteins: an approach for stereospecific NMR assignments of CH3 groups in Val and Leu residues.
Related Articles Selective 'unlabeling' of amino acids in fractionally 13C labeled proteins: an approach for stereospecific NMR assignments of CH3 groups in Val and Leu residues.
J Biomol NMR. 2001 Mar;19(3):267-72
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A novel methodology for stereospecific NMR assignments of methyl (CH3) groups of Val and Leu residues in fractionally 13C-labeled proteins is...
NMR Structure Determinations of Small Proteins Using only One Fractionally 20% 13C- and Uniformly 100% 15N-Labeled Sample.
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