Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins-Reference-Cited by-同舟云学术

Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins

Published:2018-10-05 Issue:10 Volume:4 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Jemth Per¹^ORCID,Karlsson Elin¹,Vögeli Beat²^ORCID,Guzovsky Brenda³,Andersson Eva¹,Hultqvist Greta⁴^ORCID,Dogan Jakob⁵,Güntert Peter⁶⁷⁸^ORCID,Riek Roland⁶,Chi Celestine N.¹^ORCID

Affiliation:

1. Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, SE-75123 Uppsala, Sweden.

2. Department of Biochemistry and Molecular Genetics, University of Colorado at Denver, 12801 East 17th Avenue, Aurora, CO 80045, USA.

3. Protein Physiology Lab, FCEyN-Universidad de Buenos Aires, IQUIBICEN/CONICET, Intendente Güiraldes 2160, Ciudad Universitaria, C1428EGA Buenos Aires, Argentina.

4. Department of Pharmaceutical Biosciences, Uppsala University, BMC Box 591, SE-75124 Uppsala, Sweden.

5. Department of Biochemistry and Biophysics, Stockholm University, SE-10691 Stockholm, Sweden.

6. Laboratory of Physical Chemistry, ETH Zürich, ETH-Hönggerberg, Zürich, Switzerland.

7. Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University, 60438 Frankfurt am Main, Germany.

8. Graduate School of Science, Tokyo Metropolitan University, Tokyo 192-0397, Japan.

Abstract

Structural snapshots characterize six hundred million years of evolution of intrinsically disordered proteins.

Funder

Wenner-Gren Foundation

University of Colorado Denver

Swedish Research Council Formas

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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