The complex folding network of single calmodulin molecules (Q34228218)

31 July 2017

The complex folding network of single calmodulin molecules (English)

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31 July 2017

Johannes Stigler

1

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author name string

Fabian Ziegler

2

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31 July 2017

Anja Gieseke

3

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31 July 2017

J Christof M Gebhardt

4

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31 July 2017

Matthias Rief

5

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31 July 2017

language of work or name

English

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publication date

1 October 2011

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31 July 2017

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31 July 2017

334

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31 July 2017

512-516

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31 July 2017

6055

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Theory of protein folding

31 July 2017

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Atomic force microscopy reveals the mechanical design of a modular protein.

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Single molecule force spectroscopy reveals that electrostatic interactions affect the mechanical stability of proteins

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Ligand-dependent equilibrium fluctuations of single calmodulin molecules

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The folding cooperativity of a protein is controlled by its chain topology

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Direct observation of the three-state folding of a single protein molecule

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Full distance-resolved folding energy landscape of one single protein molecule

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Direct measurement of the full, sequence-dependent folding landscape of a nucleic acid

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Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins

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Ligand binding and thermodynamic stability of a multidomain protein, calmodulin

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Protein structure by mechanical triangulation

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Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy: evidence for interaction between the two globular domains.

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Force unfolding kinetics of RNA using optical tweezers. II. Modeling experiments.

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Direct observation of active protein folding using lock-in force spectroscopy

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The gated gait of the processive molecular motor, myosin V.

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Reconstitution of Calmodulin from Domains and Subdomains: Influence of Target Peptide

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Slow Conformational Dynamics and Unfolding of the Calmodulin C-Terminal Domain

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Identifiers

DOI

10.1126/SCIENCE.1207598

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31 July 2017

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