Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding. - Wikidata - awgldk - TriplyDB

Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.

Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.

http://www.wikidata.org/entity/Q41821911

about

Tryptophan-tryptophan energy transfer and classification of tryptophan residues in proteins using a therapeutic monoclonal antibody as a model.Illuminating the off-pathway nature of the molten globule folding intermediate of an α-β parallel protein.Fluorescence of Alexa fluor dye tracks protein folding.Folding of proteins with a flavodoxin-like architecture.The Ribosome Restrains Molten Globule Formation in Stalled Nascent Flavodoxin Exploring the structure of the N-terminal domain of CP29 with ultrafast fluorescence spectroscopy.Digalactosyl-diacylglycerol-deficiency lowers the thermal stability of thylakoid membranes.5-fluorotryptophan as dual probe for ground-state heterogeneity and excited-state dynamics in apoflavodoxin.Keeping time: could quantum beating in microtubules be the basis for the neural synchrony related to consciousness?FRET studies of various conformational states adopted by transthyretin.Materials for FRET Analysis: Beyond Traditional Dye-Dye Combinations

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P2860

Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.

http://www.wikidata.org/entity/Q41821911

description

2008 nî lūn-bûn

@nan

2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

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2008年论文

@zh-cn

name

Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.

@en

type

label

Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.

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prefLabel

Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.

@en

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BIOPHYSJ.108.132001

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Biophysical Journal

P1476

Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding.

@en

P2093

Adrie H Westphal

http://www.w3.org/2001/XMLSchema#string

Antonie J W G Visser

http://www.w3.org/2001/XMLSchema#string

Arie van Hoek

http://www.w3.org/2001/XMLSchema#string

Carlo P M van Mierlo

http://www.w3.org/2001/XMLSchema#string

Herbert van Amerongen

http://www.w3.org/2001/XMLSchema#string

Nina V Visser

http://www.w3.org/2001/XMLSchema#string

P2860

Mechanisms of tryptophan fluorescence shifts in proteins

From Levinthal to pathways to funnels

A structural census of genomes: comparing bacterial, eukaryotic, and archaeal genomes in terms of protein structure.

Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.

Protein folding: progress made and promises ahead.

The folding energy landscape of apoflavodoxin is rugged: hydrogen exchange reveals nonproductive misfolded intermediates

The use of site-directed fluorophore labeling and donor-donor energy migration to investigate solution structure and dynamics in proteins.

Reassessing random-coil statistics in unfolded proteins.

Förster excitation energy transfer in peridinin-chlorophyll-a-protein.

Evidence for a novel mechanism of time-resolved flavin fluorescence depolarization in glutathione reductase.

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2462-2469

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10.1529/BIOPHYSJ.108.132001

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23175919

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18708472

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2517029

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