Z-DNA binding proteins (ZBPs) play important roles in RNA editing, innate immune responses, and viral infections. Numerous studies have implicated a role for conformational motions during ZBPs binding upon DNA, but the quantitative intrinsic conformational exchanges of ZBP have not been elucidated. To understand the correlation between the biological function and dynamic feature of the Z? domains of human ADAR1 (hZ?(ADAR1)), we have performed the ^(15)N backbone amide Carr-Purcell-Meiboom-Gill...
[NMR paper] Dynamics and Interactions of a 29 kDa Human Enzyme Studied by Solid-State NMR.
Dynamics and Interactions of a 29 kDa Human Enzyme Studied by Solid-State NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Dynamics and Interactions of a 29 kDa Human Enzyme Studied by Solid-State NMR.
J Phys Chem Lett. 2018 Mar 15;9(6):1307-1311
Authors: Vasa SK, Singh H, Rovó P, Linser R
Abstract
Solid-state NMR has been employed for characterization of a broad range of biomacromolecules and supramolecular assemblies. However, because of...
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[NMR paper] The C-terminal domain of human Cdc37 studied by solution NMR.
The C-terminal domain of human Cdc37 studied by solution NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles The C-terminal domain of human Cdc37 studied by solution NMR.
J Biomol NMR. 2015 Nov;63(3):315-21
Authors: Zhang Z, Keramisanou D, Dudhat A, Paré M, Gelis I
PMID: 26400850
[NMR paper] NMR study of the Z-DNA binding mode and B-Z transition activity of the Z? domain of human ADAR1 when perturbed by mutation on the ?3 helix and ?-hairpin.
NMR study of the Z-DNA binding mode and B-Z transition activity of the Z? domain of human ADAR1 when perturbed by mutation on the ?3 helix and ?-hairpin.
Related Articles NMR study of the Z-DNA binding mode and B-Z transition activity of the Z? domain of human ADAR1 when perturbed by mutation on the ?3 helix and ?-hairpin.
Arch Biochem Biophys. 2014 Jul 7;
Authors: Jeong M, Lee AR, Kim HE, Choi YG, Choi BS, Lee JH
Abstract
The Z? domains of human ADAR1 (Z?ADAR1) bind to Z-DNA via interaction mediated by the ?3-core and ?-hairpin....
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[NMR paper] NMR dynamics study of the Z-DNA binding domain of human ADAR1 bound to various DNA duplexes.
NMR dynamics study of the Z-DNA binding domain of human ADAR1 bound to various DNA duplexes.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR dynamics study of the Z-DNA binding domain of human ADAR1 bound to various DNA duplexes.
Biochem Biophys Res Commun. 2012 Nov 9;428(1):137-41
Authors: Lee AR, Kim HE, Lee YM, Jeong M, Choi KH, Park JW, Choi YG, Ahn HC, Choi BS, Lee JH
Abstract
The Z-DNA binding domain of human ADAR1 (Z?(ADAR1))...
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[NMR paper] NMR investigation on the DNA binding and B-Z transition pathway of the Z? domain of human ADAR1.
NMR investigation on the DNA binding and B-Z transition pathway of the Z? domain of human ADAR1.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR investigation on the DNA binding and B-Z transition pathway of the Z? domain of human ADAR1.
Biophys Chem. 2012 Dec 21;172C:18-25
Authors: Lee YM, Kim HE, Lee EH, Seo YJ, Lee AR, Lee JH
Abstract
Human ADAR1, which has two left-handed Z-DNA binding domains, preferentially binds Z-DNA rather than B-DNA with a high...
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NMR Study on the B–ZJunction Formation ofDNA Duplexes Induced by Z-DNA Binding Domain of Human ADAR1
NMR Study on the B–ZJunction Formation ofDNA Duplexes Induced by Z-DNA Binding Domain of Human ADAR1
Yeon-Mi Lee, Hee-Eun Kim, Chin-Ju Park, Ae-Ree Lee, Hee-Chul Ahn, Sung Jae Cho, Kwang-Ho Choi, Byong-Seok Choi and Joon-Hwa Lee
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja211581b/aop/images/medium/ja-2011-11581b_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja211581b
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http://feeds.feedburner.com/~r/acs/jacsat/~4/9iGipRMHcHU
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[NMR paper] Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Related Articles Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Biochemistry. 2005 May 31;44(21):7644-55
Authors: Laurents DV, Scholtz JM, Rico M, Pace CN, Bruix M
The conformational stability of ribonuclease Sa (RNase Sa) has been measured at the per-residue level by NMR-monitored hydrogen exchange at pH* 5.5 and 30 degrees C. In these conditions, the exchange mechanism was found to be EXII. The conformational stability...
Conformational exchange of the Zalpha domain of human RNA editing enzyme ADAR1 studied by NMR spectroscopy
Linear Mode
