Continuous Thermal Collapse of the Intrinsically Disordered Protein Tau Is Driven by Its Entropic Flexible Domain-Reference-Cited by-同舟云学术

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Continuous Thermal Collapse of the Intrinsically Disordered Protein Tau Is Driven by Its Entropic Flexible Domain

Published:2012-09-04 Issue:37 Volume:28 Page:13405-13410
ISSN:0743-7463
Container-title:Langmuir
language:en
Short-container-title:Langmuir

Author:

Ciasca Gabriele¹,Campi Gaetano²,Battisti Anna³,Rea Giuseppina²,Rodio Marina¹,Papi Massimiliano⁴,Pernot Petra⁵,Tenenbaum Alexander¹,Bianconi Antonio¹

Affiliation:

1. Physics Department, Sapienza University, 00185 Rome, Italy

2. Institute of Crystallography, CNR, 00015 Monterotondo, Italy

3. LISC, CMM-FBK and University of Trento, 38123 Povo, Italy

4. Institute of Physics, Catholic University, 00168 Rome, Italy

5. Structural Biology Group, ESRF, 38043 Grenoble, France

Publisher

American Chemical Society (ACS)

Subject

Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/la302628y

Reference32 articles.

1. Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins

2. Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding

3. Structural memory of natively unfolded tau protein detected by small-angle X-ray scattering

4. How fast is protein hydrophobic collapse?

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