Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins. - Wikidata - wikimedia - TriplyDB

Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins.

Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins.

http://www.wikidata.org/entity/Q38932283

about

Membrane proteins scrambling through a folding landscape.Rapid Characterization of a Mechanically Labile α-Helical Protein Enabled by Efficient Site-Specific Bioconjugation.Applications of Single-Molecule Methods to Membrane Protein Folding Studies.Transition Path Times Measured by Single-Molecule Spectroscopy.Communication: Coordinate-dependent diffusivity from single molecule trajectories.Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories.Single-molecule force spectroscopy of protein-membrane interactions.Editorial Overview: Single-Molecule Approaches up to Difficult Challenges in Folding and Dynamics.Nanoscale imaging and force probing of biomolecular systems using atomic force microscopy: from single molecules to living cells.Improved free-energy landscape reconstruction of bacteriorhodopsin highlights local variations in unfolding energy.Fodis: Software for Protein Unfolding Analysis.Compressive Force Spectroscopy: From Living Cells to Single Proteins.Calcium stabilizes the strongest protein fold

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P2860

Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins.

http://www.wikidata.org/entity/Q38932283

description

2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

@wuu

2017年学术文章

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2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

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2017年學術文章

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2017年學術文章

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2017年學術文章

@zh-hant

name

Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins.

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type

label

Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins.

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prefLabel

Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins.

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SCIENCE.AAH7124

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Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins

@en

P2093

Aric W Sanders

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

Devin T Edwards

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

Hao Yu

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

Matthew G W Siewny

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Thomas T Perkins

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P2860

Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy

Optimizing 1-μs-Resolution Single-Molecule Force Spectroscopy on a Commercial Atomic Force Microscope.

Molecular mechanism of vectorial proton translocation by bacteriorhodopsin

A transient and low-populated protein-folding intermediate at atomic resolution

Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane

Entropic elasticity of lambda-phage DNA

Models for the specific adhesion of cells to cells

Mechanical unfolding intermediates in titin modules.

Bacteriorhodopsin folds into the membrane against an external force.

Ligand-dependent equilibrium fluctuations of single calmodulin molecules.

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945-950

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355

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Thomas T Perkins

Devin T Edwards

Matthew G W Siewny

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2017-03-01T00:00:00Z

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28254940

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