Time-resolved fluorescence resonance energy transfer studies of DNA bending in double-stranded oligonucleotides and in DNA-protein complexes.

Time-resolved fluorescence resonance energy transfer studies of DNA bending in double-stranded oligonucleotides and in DNA-protein complexes.

Item
http://www.wikidata.org/entity/Q34622498
Changes in DNA bending and flexing due to tethered cations detected by fluorescence resonance energy transfer.Two-step mechanism for modifier of transcription 1 (Mot1) enzyme-catalyzed displacement of TATA-binding protein (TBP) from DNA.The fluorescence resonance energy transfer (FRET) gate: a time-resolved study.Fluorescence resonance energy transfer over approximately 130 basepairs in hyperstable lac repressor-DNA loops.Comparison of the effect of water release on the interaction of the Saccharomyces cerevisiae TATA binding protein (TBP) with "TATA Box" sequences composed of adenosine or inosine.Gapped DNA and cyclization of short DNA fragments.Optimal bundling of transmembrane helices using sparse distance constraintsDetermining protein-induced DNA bending in force-extension experiments: theoretical analysis.Time-resolved energy transfer in DNA sequence detection using water-soluble conjugated polymers: the role of electrostatic and hydrophobic interactions.DNA information: from digital code to analogue structure.The Potato Nucleotide-binding Leucine-rich Repeat (NLR) Immune Receptor Rx1 Is a Pathogen-dependent DNA-deforming Protein.Conformational heterogeneity in RNA polymerase observed by single-pair FRET microscopy.Identification of specific inhibitors of human RAD51 recombinase using high-throughput screening.Probing RNA structural dynamics and function by fluorescence resonance energy transfer (FRET).Native human TATA-binding protein simultaneously binds and bends promoter DNA without a slow isomerization step or TFIIB requirement.Global DNA dynamics of 8-oxoguanine repair by human OGG1 revealed by stopped-flow kinetics and molecular dynamics simulation.A new visible-light-driven photoelectrochemical biosensor for probing DNA-protein interactions.
P2860

Time-resolved fluorescence resonance energy transfer studies of DNA bending in double-stranded oligonucleotides and in DNA-protein complexes.

Item
http://www.wikidata.org/entity/Q34622498
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Time-resolved fluorescence res ...... and in DNA-protein complexes.
@ast
Time-resolved fluorescence res ...... and in DNA-protein complexes.
@en
Time-resolved fluorescence res ...... and in DNA-protein complexes.
@nl
type
label
Time-resolved fluorescence res ...... and in DNA-protein complexes.
@ast
Time-resolved fluorescence res ...... and in DNA-protein complexes.
@en
Time-resolved fluorescence res ...... and in DNA-protein complexes.
@nl
prefLabel
Time-resolved fluorescence res ...... and in DNA-protein complexes.
@ast
Time-resolved fluorescence res ...... and in DNA-protein complexes.
@en
Time-resolved fluorescence res ...... and in DNA-protein complexes.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P698
P356
P1433
P1476
Time-resolved fluorescence res ...... and in DNA-protein complexes.
@en
P2093
P2860
P304
P31
P356
P433
P478
P577
P698