Protein refolding

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Institut Pasteur, Université Paris Cité, Unit Evolutionary Biology of Microbial Cell, Paris, France (1)
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Johns Hopkins University, Department of Chemistry (1)
Leibniz Institute for Virology (LIV), Germany; Centre for Structural Systems Biology (CSSB), Germany; University of Siegen, Germany; Deutsches Elektronen-Synchrotron (DESY), Germany; European XFEL GmbH, Germany. (1)
Molecular and Systems Biology Lab (MOSYS), University of Vienna, Althanstrasse 14, 1090, Austria (1)
National Key Laboratory of Veterinary Public Health and Safety, College of Veterinary Medicine, China Agricultural University, Beijing, 100094, PR China. (1)
National Key Laboratory of Veterinary Public Health and Safety, College of Veterinary Medicine, China Agricultural University, Beijing, 100094, (1)
National Key Laboratory of Veterinary Public Health and Safety, College of Veterinary Medicine, China Agricultural University, Beijing, 100094National Key Laboratory of Veterinary Public Health and Safety, College of Veterinary Medicine, China AgriculturNational Key Laboratory of Veterinary Public Health and Safety, College of Veterinary Medicine, China Agricultural University, Beijing, 100094,al University, Beijing, 100094, (1)
Professor of Systems Microbiology Director of Chalmers Area of Advance Life Science Engineering Systems and Synthetic Biology Chalmers University of Technology Kemivägen 10 SE-412 96 Göteborg SWEDEN (1)
Professor, Chemistry, Duke University (1)
School of Life Sciences and Center for Soybean Research of the State Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Hong Kong SAR (1)
Uni Konstanz, Biology (1)
Universidad Autónoma de Querétaro (1)

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A Proteome-Wide Map of Chaperone-Assisted Protein Refolding in a Cytosol-like Milieu

The journey by which proteins navigate their energy landscapes to their native structures is complex, involving (and sometimes requiring) many cellular factors and processes operating in partnership with a given polypeptide chain’s intrinsic energy landscape. The cytosolic environment and its compl...

ORGANISM(S): Escherichia coli

2022-11-23 | PXD030869 | Pride

Protein misfolding involving entanglements provides a structural explanation for the origin of stretched-exponential refolding kinetics

Stretched-exponential protein refolding kinetics, first observed decades ago, were attributed to a nonnative ensemble of structures with parallel, non-interconverting folding pathways. However, the structural origin of the large energy barriers preventing interconversion between these folding pathwa...

ORGANISM(S): Escherichia coli

2025-03-18 | PXD053579 | Pride

Limited proteolisys mass spectrometry Stretched-exponential kinetics Refolding

NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system.

Not available

S-EPMC2776947 | biostudies-literature

Investigation of protein refolding using a fractional factorial screen: a study of reagent effects and interactions.

Not available

S-EPMC2253366 | biostudies-literature

An automatic refolding apparatus for preparative-scale protein production.

Not available

S-EPMC3459974 | biostudies-literature