|Appears in Collections:||Biological and Environmental Sciences Journal Articles|
|Peer Review Status:||Refereed|
|Title:||3D HCCH3 -TOCSY for resonance assignment of methyl-containing side chains in 13C-labeled proteins|
Price, Nicholas C
Barlow, Paul N
protein side chains
methyl-containing amino acids
Amino acids Metabolism
|Citation:||Uhrin D, Uhrinova S, Leadbeater C, Nairn J, Price NC & Barlow PN (2000) 3D HCCH3 -TOCSY for resonance assignment of methyl-containing side chains in 13C-labeled proteins. Journal of Magnetic Resonance, 142 (2), pp. 288-293. https://doi.org/10.1006/jmre.1999.1951|
|Abstract:||Two 3D experiments, (H)CCH3-TOCSY and H(C)CH3-TOCSY, are proposed for resonance assignment of methyl-containing amino acid side chains. After the initial proton–carbon INEPT step, during which either carbon or proton chemical shift labeling is achieved (t1), the magnetization is spread along the amino acid side chains by a carbon spin lock. The chemical shifts of methyl carbons are labeled (t2) during the following constant time interval. Finally the magnetization is transferred, in a reversed INEPT step, to methyl protons for detection (t3). The proposed experiments are characterized by high digital resolution in the methyl carbon dimension (t2max = 28.6 ms), optimum sensitivity due to the use of proton decoupling during the long constant time interval, and an optional removal of CH2, or CH2 and CH, resonances from the F2F3 planes. The building blocks used in these experiments can be implemented in a range of heteronuclear experiments focusing on methyl resonances in proteins. The techniques are illustrated using a 15N, 13C-labeled E93D mutant of Schizosacharomyces pombe phosphoglycerate mutase (23.7 kDa).|
|Rights:||The publisher does not allow this work to be made publicly available in this Repository. Please use the Request a Copy feature at the foot of the Repository record to request a copy directly from the author; you can only request a copy if you wish to use this work for your own research or private study.|
|Uhrin etl al.pdf||Fulltext - Published Version||129.57 kB||Adobe PDF||Under Embargo until 2997-11-30 Request a copy|
Note: If any of the files in this item are currently embargoed, you can request a copy directly from the author by clicking the padlock icon above. However, this facility is dependent on the depositor still being contactable at their original email address.
This item is protected by original copyright
Items in the Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
The metadata of the records in the Repository are available under the CC0 public domain dedication: No Rights Reserved https://creativecommons.org/publicdomain/zero/1.0/
If you believe that any material held in STORRE infringes copyright, please contact email@example.com providing details and we will remove the Work from public display in STORRE and investigate your claim.