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Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.

Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.

http://www.wikidata.org/entity/Q37723506

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On the Simulation of Two-dimensional Electronic Spectroscopy of Indole-containing Peptides.Steady-State Linear and Non-linear Optical Spectroscopy of Organic Chromophores and Bio-macromolecules.

P2860

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P2860

Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.

http://www.wikidata.org/entity/Q37723506

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 19 March 2014

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.

@en

Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.

@nl

type

label

Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.

@en

Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.

@nl

prefLabel

Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.

@en

Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.

@nl

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Journal of Physical Chemistry Letters

P1476

Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.

@en

P2093

Jin Wang

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

Jun Jiang

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

Zaizhi Lai

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

P2860

Approximate entropy as a measure of system complexity

Taming the complexity of protein folding

Designing a 20-residue protein

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core

Protein folding and misfolding

Atomic-level characterization of the structural dynamics of proteins

Exploring the aggregation propensity of γS-crystallin protein variants using two-dimensional spectroscopic tools

Simulation study of chiral two-dimensional ultraviolet spectroscopy of the protein backbone.

Ultrafast tryptophan-to-heme electron transfer in myoglobins revealed by UV 2D spectroscopy.

Transient 2D IR spectroscopy of ubiquitin unfolding dynamics

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1341-1346

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scholarly article

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10.1021/JZ5002264

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8

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5

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2014-03-19T00:00:00Z

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262113283

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24803996

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protein folding

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3999791

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