about
A flash in the pan: dissecting dynamic amyloid intermediates using fluorescenceFunction and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescenceNative and unfolded states of phosphoglycerate kinase studied by single-molecule FRET.Immobilization of proteins for single-molecule fluorescence resonance energy transfer measurements of conformation and dynamics.Single molecule characterization of α-synuclein in aggregation-prone states.Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins.Anchoring intrinsically disordered proteins to multiple targets: lessons from N-terminus of the p53 protein.The conformational ensembles of α-synuclein and tau: combining single-molecule FRET and simulations.Single-Molecule Analysis of Cytochrome c Folding by Monitoring the Lifetime of an Attached Fluorescent Probe.Biophysical characterization of intrinsically disordered proteins.Single molecules as optical nanoprobes for soft and complex matter.How, when and why proteins collapse: the relation to folding.Measuring distances within unfolded biopolymers using fluorescence resonance energy transfer: The effect of polymer chain dynamics on the observed fluorescence resonance energy transfer efficiency.Microsecond protein dynamics observed at the single-molecule level.Slow Interconversion in a Heterogeneous Unfolded-State Ensemble of Outer-Membrane Phospholipase A.Structural evaluations of tau protein conformation: methodologies and approaches.Colorimetric and fluorometric monitoring of the helix composition of collagen-like peptides at the nM level.
P2860
Q26997922-CB322D5A-CAD7-400F-AA2B-1525BC5E5934Q27026292-C914D559-A323-42D2-9649-B976E658E89EQ30400065-FEFAF8D6-061D-4D67-A812-388D442BCD52Q30419524-79538210-9CE8-447D-A825-827DDAD61318Q34250768-A5E88A22-C0D5-458A-83EE-40A3FD73F3FEQ34786728-C405A4E3-DB6A-4ADB-9285-0D12A89F6816Q34875111-160546B9-33FD-473A-9B4B-160008FB5D0DQ36379177-3C3F5387-A038-4F98-B463-6E7AD9FA0A82Q37217971-F744069F-8FE2-4D54-992A-5D92B306989CQ37375367-86041526-3D8A-475E-81D4-74F3C004227DQ37669308-6A8BDF0F-FEFE-4E1C-81C5-0CC9B18FCE9AQ37959224-341EA414-5B12-4914-B322-282E0547EF51Q41868708-B1A13351-0E5A-4FAE-B190-24F3FC9407A4Q42354290-0AB6B2DD-415A-4272-9CCF-FEFD01790AA6Q50577647-D7B327D7-E759-4032-92E0-F5D7A86CA09BQ51104104-994C143D-34F9-4D79-A0E3-B4E77FC2150AQ51597322-1E50BB59-6D3C-48DB-905A-FC78D21FE5D8
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 12 August 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Fluorescence characterization of denatured proteins.
@en
Fluorescence characterization of denatured proteins.
@nl
type
label
Fluorescence characterization of denatured proteins.
@en
Fluorescence characterization of denatured proteins.
@nl
prefLabel
Fluorescence characterization of denatured proteins.
@en
Fluorescence characterization of denatured proteins.
@nl
P2860
P1476
Fluorescence characterization of denatured proteins.
@en
P2093
Elizabeth Rhoades
Huimin Chen
P2860
P304
P356
10.1016/J.SBI.2008.06.008
P577
2008-08-12T00:00:00Z