Protein quaternary structures in solution are a mixture of multiple forms

Author:

Marciano Shir1,Dey Debabrata1,Listov Dina1,Fleishman Sarel J.1,Sonn-Segev Adar2,Mertens Haydyn3ORCID,Busch Florian4,Kim Yongseok4,Harvey Sophie R.4ORCID,Wysocki Vicki H.4,Schreiber Gideon1ORCID

Affiliation:

1. Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel

2. Refeyn Ltd, 1 Electric Avenue, Ferry Hinksey Road, Oxford OX2 0BY, UK

3. Hamburg Outstation, European Molecular Biology Laboratory, Notkestrasse 85, Hamburg, 22607, Germany

4. Department of Chemistry and Biochemistry, Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH, 43210, USA

Abstract

Comparing the different methods for determining oligomerization composition of a protein in solution at different concentrations. The ruler of μg ml−1 represents protein concentrations applicable for the different methods.

Funder

Israel Science Foundation

National Institutes of Health

Horizon 2020

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Reference77 articles.

1. Structural Symmetry and Protein Function

2. E. D.Levy and S.Teichmann , Structural, evolutionary, and assembly principles of protein oligomerization , Progress in Molecular Biology and Translational Science , Academic Press , 2013 , vol. 117 , pp. 25–51

3. A hydrophobic ratchet entrenches molecular complexes

4. Origin of complexity in haemoglobin evolution

5. The power of two: protein dimerization in biology

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