Ultrafast conformational dynamics in cyclic azobenzene peptides of increased flexibility. - Wikidata - wikimedia - TriplyDB

Ultrafast conformational dynamics in cyclic azobenzene peptides of increased flexibility.

Ultrafast conformational dynamics in cyclic azobenzene peptides of increased flexibility.

http://www.wikidata.org/entity/Q40278281

about

Spectroscopic studies of protein folding: linear and nonlinear methods Alpha-helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy.Light-triggered beta-hairpin folding and unfolding Azobenzene as conformational switch in model peptides.Photoisomerization in different classes of azobenzene.Connectivity matters - ultrafast isomerization dynamics of bisazobenzene photoswitches.Photoinduced conformational dynamics of a photoswitchable peptide: a nonequilibrium molecular dynamics simulation study.A conformational two-state peptide model system containing an ultrafast but soft light switch.Following the energy transfer in and out of a polyproline-peptide.Excitation mechanism in the photoisomerization of a surface-bound azobenzene derivative: Role of the metallic substrate.Ultrafast Spectroscopy of Hydroxy-Substituted Azobenzenes in Water.A combined optical and EPR spectroscopy study: azobenzene-based biradicals as reversible molecular photoswitches.

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P2860

Ultrafast conformational dynamics in cyclic azobenzene peptides of increased flexibility.

http://www.wikidata.org/entity/Q40278281

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年論文

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2004年论文

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2004年论文

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2004年论文

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name

Ultrafast conformational dynamics in cyclic azobenzene peptides of increased flexibility.

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type

label

Ultrafast conformational dynamics in cyclic azobenzene peptides of increased flexibility.

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prefLabel

Ultrafast conformational dynamics in cyclic azobenzene peptides of increased flexibility.

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Biophysical Journal

P1476

Ultrafast conformational dynamics in cyclic azobenzene peptides of increased flexibility

@en

P2093

B Fonrobert

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

C Renner

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

D Oesterhelt

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

H Satzger

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

J Wachtveitl

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

R Behrendt

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

S Spörlein

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P2860

Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution

From Levinthal to pathways to funnels

The energy landscapes and motions of proteins

Photomodulation of conformational states. III. Water-soluble bis-cysteinyl-peptides with (4-aminomethyl) phenylazobenzoic acid as backbone constituent.

Helix formation via conformation diffusion search

Elementary steps in protein folding.

Ultrafast spectroscopy reveals subnanosecond peptide conformational dynamics and validates molecular dynamics simulation.

Photoresponsive cyclic bis(cysteinyl)peptides as catalysts of oxidative protein folding.

Picosecond conformational transition and equilibration of a cyclic peptide.

Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin.

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2350-2362

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10.1016/S0006-3495(04)74292-7

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4

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1304084

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