Related ArticlesNMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Z? domains of yatapoxvirus E3L.
FEBS Lett. 2010 Oct 8;
Authors: Lee EH, Seo YJ, Ahn HC, Kang YM, Kim HE, Lee YM, Choi BS, Lee JH
The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus, consists of two domains: an N-terminal Z-DNA binding domain and a C-terminal RNA binding domain. The crystal structure of the E3L orthologue of YLDV (yabZ?(E3L)) bound to Z-DNA revealed that the overall structure of yabZ?(E3L) and its interaction with Z-DNA are very similar to those of hZ?(ADAR1). Here we have performed NMR hydrogen exchange experiments on the complexes between yabZ?(E3L) and d(CGCGCG)(2) with a variety of protein-to-DNA molar ratios. This study revealed that yabZ?(E3L) could efficiently change the B-form helix of the CG6 to left-handed Z-DNA via the active-mono B-Z transition pathway like hZ?(ADAR1).
PMID: 20937275 [PubMed - as supplied by publisher]
[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...
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11-25-2010 08:21 PM
[NMR paper] Evidence for a strong hydrogen bond in the catalytic dyad of transition-state analogu
Evidence for a strong hydrogen bond in the catalytic dyad of transition-state analogue inhibitor complexes of chymotrypsin from proton-triton NMR isotope shifts.
Related Articles Evidence for a strong hydrogen bond in the catalytic dyad of transition-state analogue inhibitor complexes of chymotrypsin from proton-triton NMR isotope shifts.
J Am Chem Soc. 2002 Apr 24;124(16):4196-7
Authors: Westler WM, Frey PA, Lin J, Wemmer DE, Morimoto H, Williams PG, Markley JL
We present here the first accurate measurements of 1H (H) versus 3H (T) isotope...
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11-24-2010 08:49 PM
[NMR paper] Ligand-induced strain in hydrogen bonds of the c-Src SH3 domain detected by NMR.
Ligand-induced strain in hydrogen bonds of the c-Src SH3 domain detected by NMR.
Related Articles Ligand-induced strain in hydrogen bonds of the c-Src SH3 domain detected by NMR.
J Mol Biol. 2000 Dec 8;304(4):497-505
Authors: Cordier F, Wang C, Grzesiek S, Nicholson LK
Changes in the molecular conformation of proteins can result from a variety of perturbations, and can play crucial roles in the regulation of biological activity. A new solution NMR method has been applied to monitor ligand-induced changes in hydrogen bond geometry in the...
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11-19-2010 08:29 PM
[NMR paper] 1H NMR study of dynamics and thermodynamics of acid-alkaline transition in ferric hem
1H NMR study of dynamics and thermodynamics of acid-alkaline transition in ferric hemoglobin of a midge larva (Tokunagayusurika akamusi).
Related Articles 1H NMR study of dynamics and thermodynamics of acid-alkaline transition in ferric hemoglobin of a midge larva (Tokunagayusurika akamusi).
Biochim Biophys Acta. 1998 Jun 11;1385(1):89-100
Authors: Koshikawa K, Yamamoto Y, Kamimura S, Matsuoka A, Shikama K
One of the components of hemoglobin from the larval hemolyph of Tokunagayusurika akamusi possesses naturally occurring substitution at the...
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11-17-2010 11:06 PM
[NMR paper] Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium
Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR.
Protein Sci. 1996 Jun;5(6):1060-6
...
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08-22-2010 02:27 PM
[NMR paper] Mechanism of hydrogen-deuterium exchange in trp repressor studied by 1H-15N NMR.
Mechanism of hydrogen-deuterium exchange in trp repressor studied by 1H-15N NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Mechanism of hydrogen-deuterium exchange in trp repressor studied by 1H-15N NMR.
J Mol Biol. 1995 Nov 3;253(4):576-89
Authors: Finucane MD, Jardetzky O
Amide proton exchange rates have been measured for fast-exchanging amides in trp aporepressor, and compared with the rates measured in the holorepressor. The results indicate that the presence...
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08-22-2010 03:50 AM
[NMR paper] Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--arjournals.annualreviews.org-images-AnnualReviews100x25.gif Related Articles Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
Annu Rev Biophys Biomol Struct. 1992;21:243-65
Authors: Englander SW, Mayne L
HX-labeling experiments in the pH-pulse mode show that protein folding can be remarkably fast. A near-native form can be reached within milliseconds. Experimental analysis of...
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08-21-2010 11:41 PM
[NMR paper] Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR
Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR.
Related Articles Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR.
Biochemistry. 1990 Nov 20;29(46):10433-7
Authors: Jeng MF, Englander SW, Elöve GA, Wand AJ, Roder H
Hydrogen exchange and two-dimensional nuclear magnetic resonance (2D NMR) techniques were used to characterize the structure of oxidized horse cytochrome c at acid pH and high ionic strength. Under these conditions, cytochrome c is known to assume a...