Minimalist probes for studying protein dynamics: thioamide quenching of selectively excitable fluorescent amino acids.
about
What We Talk About When We Talk About LightFluorogenic small molecules requiring reaction with a specific protein to create a fluorescent conjugate for biological imaging-what we know and what we need to learnEvidence for small-molecule-mediated loop stabilization in the structure of the isolated Pin1 WW domainThe effects of thioamide backbone substitution on protein stability: a study in α-helical, β-sheet, and polyproline II helical contextsEfficient synthesis and in vivo incorporation of acridon-2-ylalanine, a fluorescent amino acid for lifetime and Förster resonance energy transfer/luminescence resonance energy transfer studies.The broken ring: reduced aromaticity in Lys-Trp cations and high pH tautomer correlates with lower quantum yield and shorter lifetimesSynthesis of thioester peptides for the incorporation of thioamides into proteins by native chemical ligation.Labeling proteins with fluorophore/thioamide Förster resonant energy transfer pairs by combining unnatural amino acid mutagenesis and native chemical ligationRibosome-Mediated Incorporation of Dipeptides and Dipeptide Analogues into Proteins in Vitro.Improving target amino acid selectivity in a permissive aminoacyl tRNA synthetase through counter-selection.Efficient, Traceless Semi-Synthesis of α-Synuclein Labeled with a Fluorophore/Thioamide FRET PairKinetics of endophilin N-BAR domain dimerization and membrane interactions.Insights into the mechanism of peptide cyclodehydrations achieved through the chemoenzymatic generation of amide derivatives.Electronic interactions of i, i + 1 dithioamides: increased fluorescence quenching and evidence for n-to-π* interactionsChemoselective modifications for the traceless ligation of thioamide-containing peptides and proteinsThioamide-based fluorescent protease sensorsEndothioxopeptides: A conformational overview.Minimalist IR and fluorescence probes of protein function.Recent advances in the synthesis and application of fluorescent α-amino acids.Dimethylamine as the key intermediate generated in situ from dimethylformamide (DMF) for the synthesis of thioamides.Thioamides: versatile bonds to induce directional and cooperative hydrogen bonding in supramolecular polymers.On the use of thioamides as fluorescence quenching probes for tracking protein folding and stability.New insight into probe-location dependent polarity and hydration at lipid/water interfaces: comparison between gel- and fluid-phases of lipid bilayers.All-Thioamidated Homo-α-Peptides: Synthesis and Conformation
P2860
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P2860
Minimalist probes for studying protein dynamics: thioamide quenching of selectively excitable fluorescent amino acids.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Minimalist probes for studying ...... table fluorescent amino acids.
@ast
Minimalist probes for studying ...... table fluorescent amino acids.
@en
type
label
Minimalist probes for studying ...... table fluorescent amino acids.
@ast
Minimalist probes for studying ...... table fluorescent amino acids.
@en
prefLabel
Minimalist probes for studying ...... table fluorescent amino acids.
@ast
Minimalist probes for studying ...... table fluorescent amino acids.
@en
P2093
P2860
P356
P1476
Minimalist probes for studying ...... table fluorescent amino acids.
@en
P2093
E James Petersson
Jacob M Goldberg
Lee C Speight
Mark W Fegley
P2860
P304
P356
10.1021/JA3005094
P407
P577
2012-04-03T00:00:00Z