Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria. (Q34032661)

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9 February 2020

title

Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria (English)

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9 February 2020

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4

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9 February 2020

Yi Liang

series ordinal

5

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9 February 2020

3

Jie Chen

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9 February 2020

author name string

Ming Jiao

series ordinal

1

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9 February 2020

Hong-Tao Li

series ordinal

2

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9 February 2020

language of work or name

English

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publication date

1 August 2010

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9 February 2020

number of pages

10

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inferred from page(s)

published in

Biophysical Journal

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9 February 2020

volume

99

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9 February 2020

issue

3

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9 February 2020

page(s)

914-923

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Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm

9 February 2020

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Protein self-association in crowded protein solutions: a time-resolved fluorescence polarization study.

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The partition of solutes between buffer solutions and solutions containing hyaluronic acid

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5 July 2018

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Macromolecular crowding: an important but neglected aspect of the intracellular environment

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Polyhemoglobin-superoxide dismutase-catalase as a blood substitute with antioxidant properties

5 July 2018

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Adsorption of globular proteins on locally planar surfaces: models for the effect of excluded surface area and aggregation of adsorbed protein on adsorption equilibria

5 July 2018

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Conformational dynamics of bovine Cu, Zn superoxide dismutase revealed by time-resolved fluorescence spectroscopy of the single tyrosine residue

5 July 2018

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5 July 2018

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5 July 2018

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5 July 2018

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5 July 2018

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Structure and heme environment of beef liver catalase at 2.5 A resolution

5 July 2018

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5 July 2018

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29 October 2018

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29 October 2018

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Macromolecular crowding enhances the binding of superoxide dismutase to xanthine oxidase: implications for protein-protein interactions in intracellular environments

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12 December 2020

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Protein−Protein Interactions: Interface Structure, Binding Thermodynamics, and Mutational Analysis

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Mixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: implications for protein folding in physiological environments

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12 December 2020

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10.1016/J.BPJ.2010.05.013

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20682270%20AND%20SRC:MED&resulttype=core&format=json

9 February 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20682270%20AND%20SRC:MED&resulttype=core&format=json

9 February 2020

PubMed publication ID

20682270

1 reference