The use of singlet-singlet energy transfer to study macromolecular assemblies.
about
Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex.Proximity relationships between residue 117 of rabbit skeletal troponin-I and residues in troponin-C and actin.Application of the Dale-Eisinger analysis to proximity mapping in the contractile system.Reversible inhibition of cathepsin L-like proteases by 4-mer pseudopeptides.Dissociation of peripheral protein-membrane complexes by high pressureCD4-T-cell antigen receptor complexes on human leukemia T cells.Fluorescence changes of a label attached near the myosin active site on nucleotide binding in rat skeletal muscle fibres.Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes.FRET based quantification and screening technology platform for the interactions of leukocyte function-associated antigen-1 (LFA-1) with intercellular adhesion molecule-1 (ICAM-1).Determination of the distance between two spin labels attached to a macromolecule.Quantitation of fluorescence energy transfer between cell surface proteins via fluorescence donor photobleaching kinetics.Calculation of resonance energy transfer in crowded biological membranes.Loss of conformational stability in calmodulin upon methionine oxidationLocalization of Cys133 of rabbit skeletal troponin-I with respect to troponin-C by resonance energy transferAnalysis of nonexponential fluorescence decay data by a method of moments.Fluorescence energy transfer dye-labeled primers for DNA sequencing and analysis.RAG and HMGB1 create a large bend in the 23RSS in the V(D)J recombination synaptic complexes.Flow cytometric resonance energy transfer measurements support the association of a 95-kDa peptide termed T27 with the 55-kDa Tac peptide.Fluorescence energy transfer as a probe for nucleic acid structures and sequences.Real time kinetics of restriction endonuclease cleavage monitored by fluorescence resonance energy transfer.Folding properties of cytosine monophosphate kinase from E. coli indicate stabilization through an additional insert in the NMP binding domainThe architecture of the 12RSS in V(D)J recombination signal and synaptic complexes.DNA double staining for a fluorescence energy transfer study of chromatin in liver cells.Differential sensing for the regio- and stereoselective identification and quantitation of glycerides.The estimation of distances between specific backbone-labeled sites in DNA using fluorescence resonance energy transferFluorescence resonance energy transfer analysis of recombination signal sequence configuration in the RAG1/2 synaptic complex.Detection of actin assembly by fluorescence energy transferObserving the helical geometry of double-stranded DNA in solution by fluorescence resonance energy transfer.Conformational dynamics of titin PEVK explored with FRET spectroscopy.Tropomyosin dynamics in cardiac thin filaments: a multisite forster resonance energy transfer and anisotropy study.Cassette labeling for facile construction of energy transfer fluorescent primers.Distance between substrate sites on the Na-glucose cotransporter by fluorescence energy transfer.Quantification of protein-lipid selectivity using FRET.A fluorescence-quenched chitopentaose for the study of endo-chitinases and chitobiosidases.23S rRNA assisted folding of cytoplasmic malate dehydrogenase is distinctly different from its self-folding.Aggregation state of melittin in lipid vesicle membranes.Singlet oxygen triplet energy transfer-based imaging technology for mapping protein-protein proximity in intact cells.Conformational changes in human serum albumin studied by fluorescence and absorption spectroscopy. Distance measurements as a function of pH and fatty acids.Resonance energy transfer evidence for two attached states of the actomyosin complex.Fluorescence energy transfer between the myosin subfragment-1 isoenzymes and F-actin in the absence and presence of nucleotides.
P2860
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P2860
The use of singlet-singlet energy transfer to study macromolecular assemblies.
description
1978 nî lūn-bûn
@nan
1978年の論文
@ja
1978年論文
@yue
1978年論文
@zh-hant
1978年論文
@zh-hk
1978年論文
@zh-mo
1978年論文
@zh-tw
1978年论文
@wuu
1978年论文
@zh
1978年论文
@zh-cn
name
The use of singlet-singlet energy transfer to study macromolecular assemblies.
@en
The use of singlet-singlet energy transfer to study macromolecular assemblies.
@nl
type
label
The use of singlet-singlet energy transfer to study macromolecular assemblies.
@en
The use of singlet-singlet energy transfer to study macromolecular assemblies.
@nl
prefLabel
The use of singlet-singlet energy transfer to study macromolecular assemblies.
@en
The use of singlet-singlet energy transfer to study macromolecular assemblies.
@nl
P1476
The use of singlet-singlet energy transfer to study macromolecular assemblies.
@en
P2093
Fairclough RH
P304
P356
10.1016/S0076-6879(78)48019-X
P407
P577
1978-01-01T00:00:00Z