DNA conformational change produced by the site-specific interstrand cross-link of trans-diamminedichloroplatinum(II)

Biochemistry ◽  
1993 ◽  
Vol 32 (43) ◽  
pp. 11676-11681 ◽  
Author(s):  
Viktor Brabec ◽  
Miroslav Sip ◽  
Marc Leng
Keyword(s):  
Conformational Change ◽  
Cross Link ◽  
Site Specific

On-demand shape transformation of polymer vesicles via site-specific isomerization of hydrazone photoswitches in monodisperse hydrophobic oligomers

2021 ◽  
Author(s):  
Valene Wang ◽  
Jiwon Kim ◽  
Junyoung Kim ◽  
Seul Woo Lee ◽  
Kyoung Taek Kim
Keyword(s):  
Drug Delivery ◽  
Block Copolymers ◽  
Conformational Change ◽  
Self Assembly ◽  
Shape Control ◽  
Shape Transformation ◽  
Site Specific ◽  
On Demand ◽  
Polymer Vesicles

The shape control of nanostructures formed by the solution self-assembly of block copolymers is of significance for drug delivery. In particular, site-specific perturbation resulting in the conformational change of the...

scholarly journals Site-specific cross-linking of proteins to DNA via a new bioorthogonal approach employing oxime ligation

2018 ◽  
Vol 54 (49) ◽  
pp. 6296-6299 ◽  
Author(s):  
Suresh S. Pujari ◽  
Yi Zhang ◽  
Shaofei Ji ◽  
Mark D. Distefano ◽  
Natalia Y. Tretyakova
Keyword(s):  
Cross Linking ◽  
Cross Link ◽  
Site Specific ◽  
Link Formation

Model site-specific DNA–protein cross-link formation by bioorthogonal oxime ligation.

Application of Site-Specific Spin Labeling for NMR Detecting Inhibitor-Induced Conformational Change of HIV-1 Reverse Transcriptase

ChemMedChem ◽  
2016 ◽  
Vol 11 (4) ◽  
pp. 363-366 ◽  
Author(s):  
Supaporn Seetaha ◽  
Maho Yagi-Utsumi ◽  
Takumi Yamaguchi ◽  
Kentaro Ishii ◽  
Supa Hannongbua ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Conformational Change ◽  
Spin Labeling ◽  
Site Specific ◽  
Hiv 1

scholarly journals Mechanism by Which Exosites Promote the Inhibition of Blood Coagulation Proteases by Heparin-activated Antithrombin

2007 ◽  
Vol 282 (46) ◽  
pp. 33609-33622 ◽  
Author(s):  
Gonzalo Izaguirre ◽  
Richard Swanson ◽  
Srikumar M. Raja ◽  
Alireza R. Rezaie ◽  
Steven T. Olson
Keyword(s):  
Blood Coagulation ◽  
Conformational Change ◽  
Blood Clotting ◽  
Factor Xa ◽  
Kinetic Studies ◽  
Complex Interaction ◽  
Wild Type ◽  
Site Specific ◽  
Equilibrium Binding ◽  
Diffusion Controlled

Heparin activates the serpin, antithrombin, to inhibit its target blood-clotting proteases by generating new protease interaction exosites. To resolve the effects of these exosites on the initial Michaelis docking step and the subsequent acylation and conformational change steps of antithrombin-protease reactions, we compared the reactions of catalytically inactive S195A and active proteases with site-specific fluorophore-labeled antithrombins that allow monitoring of these reaction steps. Heparin bound to N,N′-dimethyl-N-(acetyl)-N′-(7-nitrobenz-3-oxa-1,3-diazol-4-yl)ethylenediamine (NBD)-fluorophore-labeled antithrombins and accelerated the reactions of the labeled inhibitor with thrombin and factor Xa similar to wild type. Equilibrium binding of NBD-labeled antithrombins to S195A proteases showed that exosites generated by conformationally activating antithrombin with a heparin pentasaccharide enhanced the affinity of the serpin for S195A factor Xa minimally 100-fold. Moreover, additional bridging exosites provided by a hexadecasaccharide heparin activator enhanced antithrombin affinity for both S195A factor Xa and thrombin at least 1000-fold. Rapid kinetic studies showed that these exosite-mediated enhancements in Michaelis complex affinity resulted from increases in kon and decreases in koff and caused antithrombin-protease reactions to become diffusion-controlled. Competitive binding and kinetic studies with exosite mutant antithrombins showed that Tyr-253 was a critical mediator of exosite interactions with S195A factor Xa; that Glu-255, Glu-237, and Arg-399 made more modest contributions to these interactions; and that exosite interactions reduced koff for the Michaelis complex interaction. Together these results show that exosites generated by heparin activation of antithrombin function both to promote the formation of an initial antithrombin-protease Michaelis complex and to favor the subsequent acylation of this complex.

scholarly journals Insights into DNA Platination within Unusual Structural Settings

2011 ◽  
Vol 2011 ◽  
pp. 1-17
Author(s):  
Stephanie Harvie ◽  
Owen Wilson ◽  
John A. Parkinson
Keyword(s):  
Nucleic Acid ◽  
Nmr Spectroscopy ◽  
Nucleic Acids ◽  
Product Formation ◽  
Loop Formation ◽  
Hairpin Loop ◽  
Cross Link ◽  
Site Specific ◽  
Phosphodiester Backbone ◽  
Dna Platination

2D HSQC NMR spectroscopy has been used to monitor reaction and product formation between and nucleic acids possessing irregular topologies and containing site-specific phosphorothioate substitution in the phosphodiester backbone. Comparison of the reaction profiles of dimer nucleic acids with and without phosphorothioate substitution is made with their short nucleic acid counterparts containing the key dimer components. Whereas d(GpA) is relatively unreactive towards , NMR evidence suggests that the tandem sheared mismatch duplex d(GCG3pAGC)2 reacts to form the head-to-tail interstrand G3-N7-Pt-G3-N7 cross-link. The equivalent phosphorothioate R,S-d(GsA) reacts to form a monoiodo, monosulphur adduct, whereas the tandem sheared mismatch phosphorothioate duplex d(GCGsAG5C)2 (VIs) reacts to form the unusual intrastrand macrochelate , in which platinum is attached at both sulphur and G5-N7. Experimental evidence supports the formation of a stabilized mismatch duplex in which platinum is attached to two nitrogen centres in the sequence d(CGCGpTGCG) in contrast to R,S-d(CGCGsT5GCG) for which NMR evidence supports macrochelate-stabilized hairpin loop formation cross-linked at both phosphorothioate sulphur and T5-N3.

scholarly journals Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link

2004 ◽  
Vol 101 (16) ◽  
pp. 5940-5945 ◽  
Author(s):  
M. Guo ◽  
B. Bhaskar ◽  
H. Li ◽  
T. P. Barrows ◽  
T. L. Poulos
Keyword(s):  
Crystal Structure ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Cross Link ◽  
Site Specific
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