Ensemble FRET methods in studies of intrinsically disordered proteins.

Ensemble FRET methods in studies of intrinsically disordered proteins.

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http://www.wikidata.org/entity/Q38023722
Computational approaches for inferring the functions of intrinsically disordered proteinsA flash in the pan: dissecting dynamic amyloid intermediates using fluorescenceOn the energy components governing molecular recognition in the framework of continuum approachesFörster resonance energy transfer: Role of diffusion of fluorophore orientation and separation in observed shifts of FRET efficiency.Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis.Finding Our Way in the Dark Proteome.Structural Rearrangement from Oligomer to Fibril Detected with FRET in a Designed Amphiphilic Peptide.High-resolution structural characterization of Noxa, an intrinsically disordered protein, by microsecond molecular dynamics simulations.Characterizing highly dynamic conformational states: The transcription bubble in RNAP-promoter open complex as an example.
P2860

Ensemble FRET methods in studies of intrinsically disordered proteins.

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http://www.wikidata.org/entity/Q38023722
description
article científic
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article scientifique
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articol științific
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articolo scientifico
@it
artigo científico
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artigo científico
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artigo científico
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artikel ilmiah
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artikull shkencor
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artículo científico
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name
Ensemble FRET methods in studies of intrinsically disordered proteins.
@en
type
label
Ensemble FRET methods in studies of intrinsically disordered proteins.
@en
prefLabel
Ensemble FRET methods in studies of intrinsically disordered proteins.
@en
P1433
P1476
P2093
P304
P31
P356
P407
P478
P577
P698
P356
P1433
P1476
Ensemble FRET methods in studies of intrinsically disordered proteins.
@en
P2093
P304
P31
P356
10.1007/978-1-61779-927-3_28
P407
P478
P577
P698