DBD Dyes As Fluorescence Lifetime Probes To Study Conformational Changes In Proteins

Below is result for DBD Dyes As Fluorescence Lifetime Probes To Study Conformational Changes In Proteins in PDF format. You can download or read online all document for free, but please respect copyrighted ebooks. This site does not host PDF files, all document are the property of their respective owners.

Replication Protein A Mediated G-Quadruplex Unfolding A

by MH Qureshi 2013 between two fluorescent dye molecules, termed as a donor and acceptor. In FRET, an interacting partners or its own conformational changes.

Contribution of advanced fluorescence microscopy - UCL

by SW Botchway 2021 Cited by 1 ly fluorescence lifetime imaging (FLIM) and super- resolution microscopy (SRM). This allows for conformational changes. (Suhling et al.

The Pennsylvania State University The Graduate - ETDA

by LF Mottram 2007 As a non-fluorescent molecular probe of potential drug targets and the steroid dephosphorylates NFAT, causing a conformational change that unmasks.

This is the pre-print version of the following book - Digibug

Wessig P (2013) DBD dyes as fluorescence lifetime probes to study conformational changes in proteins. Chemistry. (Easton). 19:17349 17357.57 pages

Review of fluorescent steroidal ligands for the estrogen

by N Gajadeera 2019 Cited by 6 statement suggests, the proteins used in these studies were not the intact [68] Reaction with activated fluorescent dyes gave the desired probes.

14-3-3 Protein Masks the DNA Binding Interface of Forkhead

by J Silhan 2009 Cited by 61 ing, however, does not cause any dramatic conformational change of FOXO4 as documented by the results of tryptophan fluorescence experiments 

Dynamics and Selective Remodeling of the DNA-binding

by N Pokhrel 2019 Cited by 33 cerevisiae RPA and visualized the conformational dynamics of DBD-AMB543 and RPA DBD-DMB543 produce a change in fluorescence intensity.

Structural basis for DNA recognition and allosteric control of

by J Osz 2020 Cited by 3 The appearance of multiple lifetimes as a result of conformation- and context- dependent quenching of fluorescent probes in proteins is a common 

Biophysical Investigations into the Structural Dynamics of

Chromophore photochemistry and protein conformational changes tools, fluorescent proteins and biosensors, and light-responsive biomaterials 60.

Mesoscopic protein-rich clusters host the nucleation of mutant

by DS Yanga 2021 Cited by 1 Fig. 1. The R248Q mutation and aggregation on p53 R248Q in breast cancer cells. (A) The structure of the DBD (94 to 292) 

An automated fluorescence lifetime imaging multiwell plate

by DJ Kelly Cited by 2 2.2.1 Biological applications of fluorescent dyes interactions, changes in protein conformation, DNA hybridisation) are inaccessible to traditional.266 pages

Identification of a PU.1 IRF4 protein interaction - PNAS

by SR McKercher 2003 Cited by 16 IRF4 DBD to DNA, in the absence of PU.1, was reported when cysteine to attach a fluorescent probe to test for protein protein.


by AO Baldridge 2011 throughout my studies at Georgia Tech have contributed to the research 8 Recapture of Fluorescence in a Protein Host: Probe Development Using GFP.


We found that they bind the fluorescent dye 4,4. -dianilino-1 Our findings support the use of single-Trp fluorescence as a probe for evaluating p53 stability, thermodynamically ​stability of the p53 DBD, due to the loss of interactions that maintains fluorescence measurements to detect changes in protein conformation.

Final Thesis 05-03-08c - Edinburgh Research Archive

by EM Graham 2008 Cited by 1 A molecular probe with a solvent-sensitive fluorescence lifetime has been providing a stimulating and fun environment in which to learn and grow.

A FRET Investigation toward a Liposome-Based Assay

by HT Hoang 2018 Cited by 1 DBD Dyes as Fluorescence. Lifetime Probes to Study Conformational Changes in Proteins. Chem. - Eur. J. 2013, 19 (51), 17349−17357. (4) Wessig, 

Time-Varying Excitation in Fluorescence Spectroscopy - DiVA

by registration of changes in the average fluorescence intensity related Single-molecule FRET measurements can be used to study conformations of bio-.

High-throughput screening assays for the identification of

by J Inglese Cited by 630 Further, fluorescent probes can transfer energy to proteins or dyes linked by a protease consensus sequence. When expressed.

Chem Soc Rev - The Royal Society of Chemistry

10 Apr 2014 These probes are fluorescent dyes with a charge donor and a charge acceptor. surroundings, conformational changes in proteins can be.

Nanoscale REVIEW

by C Brites 2012 Cited by 1052 emission intensity and/or lifetime of dye-sensitized Pdots,29,30 conformational changes (or protonation) of one of the emitting.

Two-photon phase-resolved fluorescence-lifetime

by HNHB Mohamed 2020 This study proposes a new Fluorescence lifetime imaging microscopy (FLIM) changes in ruthenium-based dyes were recorded to quantify the 


by B Cheng 2016 opens the door for future studies of center-deep tissue fluorescence probe for the investigation of the conformation change of protein or the protein 

Tm3+-doped NaYF4 nanoparticles: upconversion - publish.UP

by A López de Guereñu 2020 4.4 Studying the energy transfer between Tm3+-doped upconverting nanoparticles. (UCNP) and an organic (DBD-6) dye

A genetically encoded fluorescent temperature - Nature

by EG Maksimov 2019 Cited by 10 The demand to study normal functioning and pathological fluorescent proteins forming a FRET pair, changes its conformation upon binding of Ca2+ ions, 

Molecular mechanisms of the pressure-activation of Mrr, a

by A Bourges 2018 Regulation of fatty acid membrane protein synthesis Figure 2.2: Structure of the fluorescent probes used in this work.

Design and Synthesis of a Fluorescent Probe with a - MDPI

by H Liu 2019 Cited by 5 In the present study, a turn-on fluorescent probe-KCP, based on lifetime probes to study conformational changes in proteins.

Characterization of a Partially Folded Monomer of the DNA

by D Foguel 1998 Cited by 42 both DNA and protein undergo conformational changes upon interaction, especially at the E2-DBD using high pressure in combination with fluorescence.

Advancing Fluorescence Fluctuation Microscopy in Living

by KH Hur 2015 protein interactions. By exploiting the brightness of fluorescence intensity fluctuations we are able to measure the stoichiometry of protein complexes.

Interaction of the anticancer p28 peptide with p53-DBD as

by AR Bizzarri 1863 Cited by 8 345 nm and the fluorescence lifetime data were acquired until the peak likely via a DBD conformational change, on the Trp fluorescence.

Coordinated Conformational Processing of the - Cell Press

by V Dahiya 2019 Cited by 26 The tumor suppressor protein p53 is a sequence-specific tran- the anisotropy change of the Cy5-DNA-p53-DBD.23 pages

Fluorescently labeled DNA probe in STORM imaging and

by C Chen 2019 Upon adding the dye-attached DNA probe, ZF proteins interacted with the DNA probe and 2.8 Total Internal Reflection Fluorescence (TIRF) Microscopy

Contribution of advanced fluorescence nano microscopy

by SW Botchway 2021 Cited by 1 fluorescence nano microscopy towards revealing mitotic chromosome structure. Chromosome Research. ly fluorescence lifetime imaging (FLIM) and super-.

Quantitative Fluorescence Microscopy of Protein Dynamics in

by S Ibrahim 2006 Cited by 2 1.2 Fluorescent Probes Visible Fluorescent proteins. 1.2.1 Fluorescence Conformational change related fluctuations in the order of milliseconds  261 pages

Bioluminescence and Fluorescence Imaging for In Vivo

complementation assays based on luciferases and fluorescent proteins, and assays based on nonradiative energy transfer (FRET and BRET).1.


by Q Chai 2016 1.1.2 Experimental Techniques in the Study of Protein Oligomerization which the click chemistry is used to attach a probe (a fluorescent dye or 

Dynamics and Selective Remodeling of the DNA - bioRxiv

4 Oct 2018 Replication protein A (RPA) coordinates important DNA metabolic events by in fluorescence intensity changes of the RPA-DBD-AMB543 ssDNA 


long distance, which allows exploring conformational changes in large sensor Ellison EH, Moodley D, Hime J (2006) Fluorescence study of arene probe 

Total Internal Reflection Fluorescence Microscopy for

The fluorescence decay rate resulting from continuous evanescent conformational change in the AF-2 domain that releases the corepressor. Coactivators 

Mesoscopic Liquid Clusters Represent a Distinct Condensate

by DS Yang Cited by 4 We establish that p53 R248Q forms mesoscopic protein- sensitivity of antibodies to their antigen to attach fluorescent dyes to specific targets within a 

Live Cell Fluorescence Imaging of Nucleotide Dynamics : ATP

by A Bhat 2021 an increase in the fluorescence lifetime of the dye. for studying the structure and conformational changes of proteins and nucleic.

Structural reorganization of the chromatin remodeling - eLife

by R Sundaramoorthy 2017 Cited by 50 promoters results in changes to gene expression (Raveh-Sadka et We first sought to study the conformation of the Chd1 protein in 

Mechanism of DNA binding of an unusual - UNSWorks

an unexpected conformational change during complex formation: The DNA molecule Chapter: GabR protein purification, fluorescent labelling and 

Dr.rer.nat. Dipl.Chem. Robert Wawrzinek - Max-Planck

2013 DBD Dyes as Fluorescence Lifetime Probes to Study Conformational Changes in Proteins. R. Wawrzinek, J. Ziomkowska, J. Heuveling, M. Mertens,  5 pages

Drug discovery technologies to identify and characterize

Among the proteins encoded by these target genes of PXR tivator peptide as the fluorescent probe that interacts with the. PXR/RXR heterodimer [34], 

Single-Molecule Analysis and Engineering of DNA - NSF-PAR

by S Mohapatra 2019 Cited by 16 the reactive linker attached to a fluorescent dye and the protein probe single-molecule conformational changes using smFRET,.


by L WU 2009 Labeling of proteins with fluorescent probes has facilitated the studies of protein twisted conformations serving as a pathway for radiationless decay.


by P Wessig shifts combined with long fluorescence lifetimes in appropriate solvents.[1, 2] In particular DBD dyes of the first generation called acyl-DBD dyes (1) are 

Quantitative Fluorescence Resonance Energy Transfer

by CP Berney 2003 Cited by 1 The same concept of FRET system has been applied to study protein-protein interaction in Moreover, the recent developments made in fluorescence lifetime.

View/Open - UCC Library and UCC researchers have made

by J Jenkins 2016 1.3.3 Fluorescent imaging dyes, probes, nanoparticles and biosensors Protein expression changes have also been studied in non-cancer cell lines.

Durham E-Theses - Durham University

by M LANDRUM 2009 Cited by 1 probes based on their fluorescent properties. used to introduce amino acid changes into proteins. Mutations are deliberately.