The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments. - Wikidata - wikimedia - TriplyDB

The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments.

The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments.

http://www.wikidata.org/entity/Q40108154

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Calcium modulates force sensing by the von Willebrand factor A2 domain Real Time FRET Based Detection of Mechanical Stress in Cytoskeletal and Extracellular Matrix Proteins Stretching to understand proteins - a survey of the protein data bank.Print your atomic force microscope.N-terminal strands of filamin Ig domains act as a conformational switch under biological forces.Fast and forceful refolding of stretched alpha-helical solenoid proteins.Single molecule force spectroscopy using polyproteins.Connecting thermal and mechanical protein (un)folding landscapes.Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulation Analyzing forced unfolding of protein tandems by ordered variates, 1: Independent unfolding times.The mechanochemistry of copper reports on the directionality of unfolding in model cupredoxin proteins.Early events in helix unfolding under external forces: a milestoning analysis.Folding and assembly of the large molecular machine Hsp90 studied in single-molecule experiments.Mechanical biochemistry of proteins one molecule at a time.Isopeptide bonds mechanically stabilize spy0128 in bacterial pili.Protein Mechanics: A New Frontier in Biomechanics.Phosphorylation facilitates the integrin binding of filamin under force Chaperone-assisted degradation: multiple paths to destruction.Single molecule mechanical manipulation for studying biological properties of proteins, DNA, and sugars.Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy.Direct observation of active protein folding using lock-in force spectroscopy.Secondary structure, mechanical stability, and location of transition state of proteins Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of I27 and ubiquitin.Free energy of membrane protein unfolding derived from single-molecule force measurements.Molecular mechanics of filamin's rod domain.Single-molecule unfolding force distributions reveal a funnel-shaped energy landscape.Dependence of protein mechanical unfolding pathways on pulling speeds.Filamin-regulated F-actin assembly is essential for morphogenesis and controls phototaxis in Dictyostelium.Nanospring behaviour of ankyrin repeats.Direct evidence of the multidimensionality of the free-energy landscapes of proteins revealed by mechanical probes.New dynamical window onto the landscape for forced protein unfolding.Protein mechanical unfolding: Importance of non-native interactions

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The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments.

http://www.wikidata.org/entity/Q40108154

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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2005年學術文章

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2005年學術文章

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The folding pathway of a fast- ...... lecule mechanical experiments.

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The folding pathway of a fast- ...... lecule mechanical experiments.

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The folding pathway of a fast- ...... lecule mechanical experiments.

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The folding pathway of a fast- ...... lecule mechanical experiments.

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Angelika A Noegel

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Ingo Schwaiger

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Matthias Rief

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Michael Schleicher

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P2860

The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold

Cellular motility driven by assembly and disassembly of actin filaments

Entropic elasticity of lambda-phage DNA

Fast kinetics and mechanisms in protein folding.

Is protein folding hierarchic? II. Folding intermediates and transition states.

Mechanical and chemical unfolding of a single protein: a comparison.

The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques

Strength of a weak bond connecting flexible polymer chains.

Pulling geometry defines the mechanical resistance of a beta-sheet protein.

Single-molecule folding.

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