Determination of the binding site size of hexaammineruthenium(iii) inside monolayers of DNA on gold

The Analyst ◽  
2021 ◽  
Author(s):  
Alireza Abi ◽  
Afsaneh Safavi
Keyword(s):  
Metal Complex ◽  
Binding Site ◽  
Dna Strands

Hexaammineruthenium(iii) metal complex can bind to surface-tethered DNA strands in excess of what is required for the compensation of the DNA charges.

Antithrombin-mediated Inhibition of Factor Vlla-Tissue Factor Complex by the Synthetic Pentasaccharide Representing the Heparin Binding Site to Antithrombin

1996 ◽  
Vol 76 (01) ◽  
pp. 005-008 ◽  
Author(s):  
Jean Claude Lormeau ◽  
Jean Pascal Herault ◽  
Jean Marc Herbert
Keyword(s):  
Binding Site ◽  
Tissue Factor ◽  
Residual Activity ◽  
Coagulation Factors ◽  
Heparin Binding ◽  
Experimental Conditions ◽  
First Order ◽  
Heparin Binding Site ◽  
Coagulant Activity

SummaryWe examined the effect of the synthetic pentasaccharide representing the minimal binding site of heparin to antithrombin on the antithrombin-mediated inactivation of factor Vila bound to tissue factor. This effect was compared to the effect of unfractionated heparin. Using purified recombinant human coagulation factors and either a clotting or an amidolytic assay for the determination of the residual activity of factor Vila, we showed that the pentasaccharide was an efficient antithrombin-dependent inhibitor of the coagulant activity of tissue factor-factor Vila complex. In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 ± 10,500 min-1 and 112,000 ± 12,000 min-1 (mean ± s.e.m., n = 3)

scholarly journals Crystallographic determination of the heme orientation and location of the cyanide binding site in yeast cytochrome c peroxidase.

1978 ◽  
Vol 253 (10) ◽  
pp. 3730-3735
Author(s):  
T.L. Poulos ◽  
S.T. Freer ◽  
R.A. Alden ◽  
N.H. Xuong ◽  
S.L. Edwards ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Binding Site ◽  
Cytochrome C Peroxidase ◽  
Cyanide Binding

scholarly journals High-Resolution Single-Molecule FRET via DNA eXchange (FRET X)

2020 ◽  
Author(s):  
Mike Filius ◽  
Sung Hyun Kim ◽  
Ivo Severins ◽  
Chirlmin Joo
Keyword(s):  
Structural Analysis ◽  
High Resolution ◽  
Single Molecule ◽  
Single Object ◽  
Single Molecule Fret ◽  
Dna Strands ◽  
Versatile Tool ◽  
Fret Efficiency ◽  
Fret Pair

ABSTRACTSingle-molecule FRET is a versatile tool to study nucleic acids and proteins at the nanometer scale. However, currently, only a couple of FRET pairs can be reliably measured on a single object. The limited number of available FRET pair fluorophores and complicated data analysis makes it challenging to apply single-molecule FRET for structural analysis of biomolecules. Currently, only a couple of FRET pairs can be reliably measured on a single object. Here we present an approach that allows for the determination of multiple distances between FRET pairs in a single object. We use programmable, transient binding between short DNA strands to resolve the FRET efficiency of multiple fluorophore pairs. By allowing only a single FRET pair to be formed at a time, we can determine the FRET efficiency and pair distance with sub-nanometer resolution. We determine the distance between other pairs by sequentially exchanging DNA strands. We name this multiplexing approach FRET X for FRET via DNA eXchange. We envision that our FRET X technology will be a tool for the high-resolution structural analysis of biomolecules and other nano-structures.

Determination of the molecular size of the 5-HT3 receptor binding site by radiation inactivation

1989 ◽  
Vol 172 (6) ◽  
pp. 497-500 ◽  
Author(s):  
H. Gozlan ◽  
L.E. Schechter ◽  
F. Bolanos ◽  
M.B. Emerit ◽  
M.C. Miquel ◽  
...  
Keyword(s):  
Binding Site ◽  
Receptor Binding ◽  
Molecular Size ◽  
Receptor Binding Site ◽  
Radiation Inactivation
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